DAP3: Difference between revisions

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{{Infobox_gene}}
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28S ribosomal protein S29, mitochondrial, also known as '''death-associated protein 3''' (DAP3), is a [[protein]] that in humans is encoded by the ''DAP3'' [[gene]] on chromosome 1.<ref name="pmid7499268">{{cite journal | vauthors = Kissil JL, Deiss LP, Bayewitch M, Raveh T, Khaspekov G, Kimchi A | title = Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death | journal = The Journal of Biological Chemistry | volume = 270 | issue = 46 | pages = 27932–6 | date = Nov 1995 | pmid = 7499268 | pmc =  | doi = 10.1074/jbc.270.46.27932 }}</ref><ref name="pmid9284927">{{cite journal | vauthors = Kissil JL, Kimchi A | title = Assignment of death associated protein 3 (DAP3) to human chromosome 1q21 by in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 77 | issue = 3–4 | pages = 252 | date = September 1997 | pmid = 9284927 | pmc =  | doi = 10.1159/000134587 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DAP3 death associated protein 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7818| accessdate = }}</ref><ref name="pmid19103604">{{cite journal | vauthors = Tang T, Zheng B, Chen SH, Murphy AN, Kudlicka K, Zhou H, Farquhar MG | title = hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis | journal = The Journal of Biological Chemistry | volume = 284 | issue = 8 | pages = 5414–24 | date = Feb 2009 | pmid = 19103604 | doi = 10.1074/jbc.M807797200 | pmc=2643507}}</ref> This gene encodes a 28S subunit protein of the [[mitochondria]]l [[ribosome]] ([[mitoribosome]]) and plays key roles in [[translation (biology)|translation]], [[cellular respiration]], and [[apoptosis]].<ref name="entrez" /><ref name="pmid19103604"/><ref name="pmid18227431">{{cite journal | vauthors = Miller JL, Koc H, Koc EC | title = Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3 | journal = Protein Science | volume = 17 | issue = 2 | pages = 251–60 | date = Feb 2008 | pmid = 18227431 | doi = 10.1110/ps.073185608 | pmc=2222727}}</ref><ref name="pmid19536094">{{cite journal | vauthors = Jacques C, Fontaine JF, Franc B, Mirebeau-Prunier D, Triau S, Savagner F, Malthiery Y | title = Death-associated protein 3 is overexpressed in human thyroid oncocytic tumours | journal = British Journal of Cancer | volume = 101 | issue = 1 | pages = 132–8 | date = Jul 2009 | pmid = 19536094 | doi = 10.1038/sj.bjc.6605111 | pmc=2713694}}</ref> Moreover, DAP3 is associated with cancer development, but has been observed to aid some cancers while suppressing others.<ref name="pmid19536094"/><ref name="pmid24300973">{{cite journal | vauthors = Jia Y, Ye L, Ji K, Zhang L, Hargest R, Ji J, Jiang WG | title = Death-associated protein-3, DAP-3, correlates with preoperative chemotherapy effectiveness and prognosis of gastric cancer patients following perioperative chemotherapy and radical gastrectomy | journal = British Journal of Cancer | volume = 110 | issue = 2 | pages = 421–9 | date = Jan 2014 | pmid = 24300973 | doi = 10.1038/bjc.2013.712 | pmc=3899757}}</ref><ref name="pmid22287761">{{cite journal | vauthors = Wazir U, Jiang WG, Sharma AK, Mokbel K | title = The mRNA expression of DAP3 in human breast cancer: correlation with clinicopathological parameters | journal = Anticancer Research | volume = 32 | issue = 2 | pages = 671–4 | date = Feb 2012 | pmid = 22287761 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Structure==
{{GNF_Protein_box
The ''DAP3'' gene encodes a 46 kDa protein located in the lower area of the small mitoribosomal subunit.<ref name="pmid18227431"/><ref name="pmid22287761"/><ref name="pmid15302871">{{cite journal | vauthors = Miyazaki T, Shen M, Fujikura D, Tosa N, Kim HR, Kon S, Uede T, Reed JC | title = Functional role of death-associated protein 3 (DAP3) in anoikis | journal = The Journal of Biological Chemistry | volume = 279 | issue = 43 | pages = 44667–72 | date = Oct 2004 | pmid = 15302871 | doi = 10.1074/jbc.M408101200 }}</ref><ref name="pmid20079882">{{cite journal | vauthors = Han MJ, Chiu DT, Koc EC | title = Regulation of mitochondrial ribosomal protein S29 (MRPS29) expression by a 5'-upstream open reading frame | journal = Mitochondrion | volume = 10 | issue = 3 | pages = 274–83 | date = Apr 2010 | pmid = 20079882 | doi = 10.1016/j.mito.2009.12.150 | pmc=2844934}}</ref> This protein contains a P-loop motif that binds GTP and a highly conserved 17-residue targeting sequence responsible for its localization to the mitochondria.<ref name="pmid18227431"/><ref name="pmid24300973"/><ref name="pmid22287761"/><ref name="pmid15302871"/> Of interest, many of the phosphorylation sites on this protein are highly conserved and clustered around GTP-binding motifs.<ref name="pmid18227431"/>
| image =
| image_source =
| PDB =  
| Name = Death associated protein 3
| HGNCid = 2673
| Symbol = DAP3
| AltSymbols =; DAP-3; DKFZp686G12159; MGC126058; MGC126059; MRP-S29; MRPS29; bMRP-10
| OMIM = 602074
| ECnumber = 
| Homologene = 3404
| MGIid = 1929538
| GeneAtlas_image1 = PBB_GE_DAP3_208822_s_at_tn.png
| Function =  
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005761 |text = mitochondrial ribosome}} {{GNF_GO|id=GO:0015935 |text = small ribosomal subunit}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0008637 |text = apoptotic mitochondrial changes}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7818
    | Hs_Ensembl = ENSG00000132676
    | Hs_RefseqProtein = NP_004623
    | Hs_RefseqmRNA = NM_004632
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 153925473
    | Hs_GenLoc_end = 153975425
    | Hs_Uniprot = P51398
    | Mm_EntrezGene = 65111
    | Mm_Ensembl = ENSMUSG00000068921
    | Mm_RefseqmRNA = NM_022994
    | Mm_RefseqProtein = NP_075370
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 89006730
    | Mm_GenLoc_end = 89035880
    | Mm_Uniprot = Q9ER88
  }}
}}
'''Death associated protein 3''', also known as '''DAP3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DAP3 death associated protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7818| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Several splice variants were observed in human [[Expressed sequence tag|ESTs]] that differ largely in the [[Five prime untranslated region|5’ UTR region]].<ref name="entrez" /><ref name="pmid20079882"/> Pseudogenes for this gene are also found in chromosomes 1 and 2.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that also participates in apoptotic pathways which are initiated by tumor necrosis factor-alpha, Fas ligand, and gamma interferon. This protein potentially binds ATP/GTP and might be a functional partner of the mitoribosomal protein S27. Splice variants that differ in the 5' UTR have been found for this gene; both variants encode the same protein. Pseudogenes corresponding to this gene are found on chromosomes 1q and 2q.<ref name="entrez">{{cite web | title = Entrez Gene: DAP3 death associated protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7818| accessdate = }}</ref>
}}


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
DAP3 is a 28S subunit protein of mitoribosomes and [[subcellular localization|localizes]] to the [[mitochondrial matrix]].<ref name="entrez" /><ref name="pmid19103604"/><ref name="pmid18227431"/> As part of the mitoribosome, DAP3 participates in the translation of the 13 [[Electron transport chain|ETC]] complex proteins encoded in the [[mitochondrial genome]], and consequently, in the regulation of cellular respiration.<ref name="entrez" /><ref name="pmid19103604"/><ref name="pmid18227431"/><ref name="pmid19536094"/> As a member of the death-associated protein ([[Death domain|DAP]]) family, DAP3 can also be found outside of the mitochondria to initiate the [[intrinsic apoptosis|extrinsic apoptotic pathway]] through its interactions with apoptotic factors, such as [[tumor necrosis factor-alpha]], [[Fas ligand]], and [[gamma interferon]].<ref name="entrez" /><ref name="pmid19103604"/><ref name="pmid24300973"/><ref name="pmid22287761"/><ref name="pmid15302871"/> Additionally, DAP3 interacts with the factor [[IPS-1]] to activate caspases 3, 8, and 9, resulting in a type of [[extracellular]] apoptosis called [[anoikis]].<ref name="pmid22287761"/><ref name="pmid15302871"/> Moreover, DAP3 may contribute to apoptosis through its mediation of mitochondrial fragmentation, as this function extends to the mediation of the [[oxidative stress]] response, [[reactive oxygen species]] (ROS) production, and ultimately, mitochondrial [[homeostasis]].<ref name="pmid19536094"/><ref name="pmid24300973"/><ref name="pmid15302871"/> DAP3 is essential for life, and its deletion in embryos is lethal.<ref name="pmid20079882"/> Nonetheless, DAP3 and its apoptotic activity can be inhibited by [[AKT]] [[phosphorylation]].<ref name="pmid22287761"/><ref name="pmid15302871"/>
 
==Clinical significance==
As aforementioned, death associated protein 3 (DAP3) has regulatory roles in [[cell respiration]] and [[apoptosis]]. Both opposites and cell respiration are important elements of cell death pathways and have underlying mechanistic roles in ischemia-reperfusion injury.<ref>{{cite journal | vauthors = Gracia-Sancho J, Casillas-Ramírez A, Peralta C | title = Molecular pathways in protecting the liver from ischaemia/reperfusion injury: a 2015 update | journal = Clinical Science | volume = 129 | issue = 4 | pages = 345–62 | date = Aug 2015 | pmid = 26014222 | doi = 10.1042/CS20150223 }}</ref><ref>{{cite journal | vauthors = Ekert PG, Vaux DL | title = The mitochondrial death squad: hardened killers or innocent bystanders? | journal = Current Opinion in Cell Biology | volume = 17 | issue = 6 | pages = 626–30 | date = Dec 2005 | pmid = 16219456 | doi = 10.1016/j.ceb.2005.09.001 }}</ref><ref name = "Kissil_1998">{{cite journal | vauthors = Kissil JL, Kimchi A | title = Death-associated proteins: from gene identification to the analysis of their apoptotic and tumour suppressive functions | journal = Molecular Medicine Today | volume = 4 | issue = 6 | pages = 268–74 | date = Jun 1998 | pmid = 9679246 | doi=10.1016/s1357-4310(98)01263-5}}</ref>
 
During a normal [[embryologic]] processes, or during cell injury (such as ischemia-reperfusion injury during [[heart attacks]] and [[strokes]]) or during developments and processes in [[cancer]], an apoptotic cell undergoes structural changes including cell shrinkage, plasma membrane blebbing, nuclear condensation, and fragmentation of the [[DNA]] and [[Cell nucleus|nucleus]]. This is followed by fragmentation into apoptotic bodies that are quickly removed by [[phagocytes]], thereby preventing an [[inflammation|inflammatory]] response.<ref>{{cite journal | vauthors = Kerr JF, Wyllie AH, Currie AR | title = Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics | journal = British Journal of Cancer | volume = 26 | issue = 4 | pages = 239–57 | date = Aug 1972 | pmid = 4561027 | doi=10.1038/bjc.1972.33 | pmc=2008650}}</ref> It is a mode of cell death defined by characteristic morphological, biochemical and molecular changes. It was first described as a "shrinkage necrosis", and then this term was replaced by apoptosis to emphasize its role opposite [[mitosis]] in tissue kinetics. In later stages of apoptosis the entire cell becomes fragmented, forming a number of plasma membrane-bounded apoptotic bodies which contain nuclear and or cytoplasmic elements. The ultrastructural appearance of [[necrosis]] is quite different, the main features being mitochondrial swelling, plasma membrane breakdown and cellular disintegration. Apoptosis occurs in many [[physiological]] and [[pathological]] processes. It plays an important role during [[embryonal]] development as programmed cell death and accompanies a variety of normal involutional processes in which it serves as a mechanism to remove "unwanted" cells.
 
DAP3 has been implicated in numerous cancers. Studies demonstrated that DAP3 expression tended to be low to nonexistent in the tumor cells of [[B-cell lymphoma]], [[non-small cell lung cancer]], [[head and neck cancer]], [[breast cancer]], [[gastric cancer]], and [[colon cancer]], possibly due to [[hypermethylation]] of the gene’s [[promoter (genetics)|promoter]].<ref name="pmid24300973"/><ref name="pmid22287761"/> Moreover, DAP3 expression has been positively correlated with improved cancer [[prognosis]], indicating that the protein combats cancer progression through its proapoptotic function.<ref name="pmid24300973"/><ref name="pmid22287761"/> As a result, DAP3 could serve as a potential [[biomarker]] to monitor the effectiveness of therapeutic treatments such as [[chemotherapy]].<ref name="pmid24300973"/>
However, in other cancers, such as [[glioblastoma multiforme]] (GBM) and [[thymoma]], DAP3 expression was found to be upregulated.<ref name="pmid19536094"/><ref name="pmid20079882"/> Thus, the specific role of DAP3 in various cancers requires further study.<ref name = "Kissil_1998"/>
 
== Interactions ==
 
DAP3 has been shown to [[Protein-protein interaction|interact]] with:
*[[DELE]],<ref name="pmid22287761"/>
*[[IPS-1]],<ref name="pmid22287761"/>
*[[AKT]],<ref name="pmid22287761"/>
*[[Protein kinase A|PKA]],<ref name="pmid20079882"/>
*[[Protein kinase C|PKC]],<ref name="pmid20079882"/>
* [[NOA1]],<ref name="pmid19103604"/><ref name="pmid20079882"/>
* [[FADD]],<ref name = pmid11376335>{{cite journal | vauthors = Miyazaki T, Reed JC | title = A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins | journal = Nature Immunology | volume = 2 | issue = 6 | pages = 493–500 | date = Jun 2001 | pmid = 11376335 | doi = 10.1038/88684 }}</ref>
* [[Glucocorticoid receptor]],<ref name = pmid10903152>{{cite journal | vauthors = Hulkko SM, Wakui H, Zilliacus J | title = The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function | journal = The Biochemical Journal | volume = 349 | issue =  3| pages = 885–93 | date = Aug 2000 | pmid = 10903152 | pmc = 1221218 | doi =  10.1042/bj3490885}}</ref>
* [[Heat shock protein 90kDa alpha (cytosolic), member A1]],<ref name = pmid10903152/> and
* [[TNFRSF10A]].<ref name = pmid11376335/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Kissil JL, Deiss LP, Bayewitch M, ''et al.'' |title=Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27932-6 |year= 1996 |pmid= 7499268 |doi= }}
* {{cite journal | vauthors = Hulkko SM, Wakui H, Zilliacus J | title = The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function | journal = Biochem. J. | volume = 349 | issue = Pt 3 | pages = 885–93 | year = 2000 | pmid = 10903152 | pmc = 1221218 | doi =  10.1042/bj3490885}}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Morgan CJ, Jacques C, Savagner F, Tourmen Y, Mirebeau DP, Malthièry Y, Reynier P | title = A conserved N-terminal sequence targets human DAP3 to mitochondria | journal = Biochem. Biophys. Res. Commun. | volume = 280 | issue = 1 | pages = 177–81 | year = 2001 | pmid = 11162496 | doi = 10.1006/bbrc.2000.4119 }}
*{{cite journal | author=Kissil JL, Kimchi A |title=Assignment of death associated protein 3 (DAP3) to human chromosome 1q21 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=77 |issue= 3-4 |pages= 252 |year= 1997 |pmid= 9284927 |doi=  }}
* {{cite journal | vauthors = Cavdar Koc E, Ranasinghe A, Burkhart W, Blackburn K, Koc H, Moseley A, Spremulli LL | title = A new face on apoptosis: death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins | journal = FEBS Lett. | volume = 492 | issue = 1–2 | pages = 166–70 | year = 2001 | pmid = 11248257 | doi = 10.1016/S0014-5793(01)02250-5 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Cavdar Koc E, Burkhart W, Blackburn K, Moseley A, Spremulli LL | title = The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present | journal = J. Biol. Chem. | volume = 276 | issue = 22 | pages = 19363–74 | year = 2001 | pmid = 11279123 | doi = 10.1074/jbc.M100727200 }}
*{{cite journal | author=Hulkko SM, Wakui H, Zilliacus J |title=The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function. |journal=Biochem. J. |volume=349 Pt 3 |issue= |pages= 885-93 |year= 2001 |pmid= 10903152 |doi= }}
* {{cite journal | vauthors = Miyazaki T, Reed JC | title = A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins | journal = Nat. Immunol. | volume = 2 | issue = 6 | pages = 493–500 | year = 2001 | pmid = 11376335 | doi = 10.1038/88684 }}
*{{cite journal | author=Morgan CJ, Jacques C, Savagner F, ''et al.'' |title=A conserved N-terminal sequence targets human DAP3 to mitochondria. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 1 |pages= 177-81 |year= 2001 |pmid= 11162496 |doi= 10.1006/bbrc.2000.4119 }}
* {{cite journal | vauthors = Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K | title = Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit | journal = J. Biol. Chem. | volume = 276 | issue = 35 | pages = 33181–95 | year = 2001 | pmid = 11402041 | doi = 10.1074/jbc.M103236200 }}
*{{cite journal | author=Cavdar Koc E, Ranasinghe A, Burkhart W, ''et al.'' |title=A new face on apoptosis: death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins. |journal=FEBS Lett. |volume=492 |issue= 1-2 |pages= 166-70 |year= 2001 |pmid= 11248257 |doi= }}
* {{cite journal | vauthors = Kenmochi N, Suzuki T, Uechi T, Magoori M, Kuniba M, Higa S, Watanabe K, Tanaka T | title = The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders | journal = Genomics | volume = 77 | issue = 1–2 | pages = 65–70 | year = 2001 | pmid = 11543634 | doi = 10.1006/geno.2001.6622 }}
*{{cite journal | author=Cavdar Koc E, Burkhart W, Blackburn K, ''et al.'' |title=The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19363-74 |year= 2001 |pmid= 11279123 |doi= 10.1074/jbc.M100727200 }}
* {{cite journal | vauthors = Berger T, Kretzler M | title = Interaction of DAP3 and FADD only after cellular disruption | journal = Nat. Immunol. | volume = 3 | issue = 1 | pages = 3–5 | year = 2002 | pmid = 11753396 | doi = 10.1038/ni0102-3b }}
*{{cite journal | author=Miyazaki T, Reed JC |title=A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins. |journal=Nat. Immunol. |volume=2 |issue= 6 |pages= 493-500 |year= 2001 |pmid= 11376335 |doi= 10.1038/88684 }}
* {{cite journal | vauthors = Hulkko SM, Zilliacus J | title = Functional interaction between the pro-apoptotic DAP3 and the glucocorticoid receptor | journal = Biochem. Biophys. Res. Commun. | volume = 295 | issue = 3 | pages = 749–55 | year = 2002 | pmid = 12099703 | doi = 10.1016/S0006-291X(02)00713-1 }}
*{{cite journal | author=Suzuki T, Terasaki M, Takemoto-Hori C, ''et al.'' |title=Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 33181-95 |year= 2001 |pmid= 11402041 |doi= 10.1074/jbc.M103236200 }}
* {{cite journal | vauthors = Berger T, Kretzler M | title = TRAIL-induced apoptosis is independent of the mitochondrial apoptosis mediator DAP3 | journal = Biochem. Biophys. Res. Commun. | volume = 297 | issue = 4 | pages = 880–4 | year = 2002 | pmid = 12359235 | doi = 10.1016/S0006-291X(02)02310-0 }}
*{{cite journal | author=Kenmochi N, Suzuki T, Uechi T, ''et al.'' |title=The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders. |journal=Genomics |volume=77 |issue= 1-2 |pages= 65-70 |year= 2001 |pmid= 11543634 |doi= 10.1006/geno.2001.6622 }}
* {{cite journal | vauthors = Zhang Z, Gerstein M | title = Identification and characterization of over 100 mitochondrial ribosomal protein pseudogenes in the human genome | journal = Genomics | volume = 81 | issue = 5 | pages = 468–80 | year = 2003 | pmid = 12706105 | doi = 10.1016/S0888-7543(03)00004-1 }}
*{{cite journal | author=Berger T, Kretzler M |title=Interaction of DAP3 and FADD only after cellular disruption. |journal=Nat. Immunol. |volume=3 |issue= 1 |pages= 3-5 |year= 2002 |pmid= 11753396 |doi= 10.1038/ni0102-3b }}
* {{cite journal | vauthors = Mukamel Z, Kimchi A | title = Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death | journal = J. Biol. Chem. | volume = 279 | issue = 35 | pages = 36732–8 | year = 2004 | pmid = 15175341 | doi = 10.1074/jbc.M400041200 }}
*{{cite journal | author=Hulkko SM, Zilliacus J |title=Functional interaction between the pro-apoptotic DAP3 and the glucocorticoid receptor. |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 3 |pages= 749-55 |year= 2002 |pmid= 12099703 |doi= }}
* {{cite journal | vauthors = Hirota T, Obara K, Matsuda A, Akahoshi M, Nakashima K, Hasegawa K, Takahashi N, Shimizu M, Sekiguchi H, Kokubo M, Doi S, Fujiwara H, Miyatake A, Fujita K, Enomoto T, Kishi F, Suzuki Y, Saito H, Nakamura Y, Shirakawa T, Tamari M | title = Association between genetic variation in the gene for death-associated protein-3 (DAP3) and adult asthma | journal = J. Hum. Genet. | volume = 49 | issue = 7 | pages = 370–5 | year = 2004 | pmid = 15179560 | doi = 10.1007/s10038-004-0161-4 }}
*{{cite journal | author=Berger T, Kretzler M |title=TRAIL-induced apoptosis is independent of the mitochondrial apoptosis mediator DAP3. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 4 |pages= 880-4 |year= 2002 |pmid= 12359235 |doi= }}
* {{cite journal | vauthors = Miyazaki T, Shen M, Fujikura D, Tosa N, Kim HR, Kon S, Uede T, Reed JC | title = Functional role of death-associated protein 3 (DAP3) in anoikis | journal = J. Biol. Chem. | volume = 279 | issue = 43 | pages = 44667–72 | year = 2004 | pmid = 15302871 | doi = 10.1074/jbc.M408101200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Sasaki H, Ide N, Yukiue H, Kobayashi Y, Fukai I, Yamakawa Y, Fujii Y | title = Arg and DAP3 expression was correlated with human thymoma stage | journal = Clin. Exp. Metastasis | volume = 21 | issue = 6 | pages = 507–13 | year = 2004 | pmid = 15679048 | doi = 10.1007/s10585-004-2153-3 }}
*{{cite journal  | author=Zhang Z, Gerstein M |title=Identification and characterization of over 100 mitochondrial ribosomal protein pseudogenes in the human genome. |journal=Genomics |volume=81 |issue= 5 |pages= 468-80 |year= 2003 |pmid= 12706105 |doi=  }}
*{{cite journal | author=Mukamel Z, Kimchi A |title=Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death. |journal=J. Biol. Chem. |volume=279 |issue= 35 |pages= 36732-8 |year= 2004 |pmid= 15175341 |doi= 10.1074/jbc.M400041200 }}
*{{cite journal | author=Hirota T, Obara K, Matsuda A, ''et al.'' |title=Association between genetic variation in the gene for death-associated protein-3 (DAP3) and adult asthma. |journal=J. Hum. Genet. |volume=49 |issue= 7 |pages= 370-5 |year= 2004 |pmid= 15179560 |doi= 10.1007/s10038-004-0161-4 }}
*{{cite journal  | author=Miyazaki T, Shen M, Fujikura D, ''et al.'' |title=Functional role of death-associated protein 3 (DAP3) in anoikis. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44667-72 |year= 2004 |pmid= 15302871 |doi= 10.1074/jbc.M408101200 }}
*{{cite journal  | author=Sasaki H, Ide N, Yukiue H, ''et al.'' |title=Arg and DAP3 expression was correlated with human thymoma stage. |journal=Clin. Exp. Metastasis |volume=21 |issue= 6 |pages= 507-13 |year= 2005 |pmid= 15679048 |doi=  }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:14, 30 August 2017

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Identifiers
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Orthologs
SpeciesHumanMouse
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28S ribosomal protein S29, mitochondrial, also known as death-associated protein 3 (DAP3), is a protein that in humans is encoded by the DAP3 gene on chromosome 1.[1][2][3][4] This gene encodes a 28S subunit protein of the mitochondrial ribosome (mitoribosome) and plays key roles in translation, cellular respiration, and apoptosis.[3][4][5][6] Moreover, DAP3 is associated with cancer development, but has been observed to aid some cancers while suppressing others.[6][7][8]

Structure

The DAP3 gene encodes a 46 kDa protein located in the lower area of the small mitoribosomal subunit.[5][8][9][10] This protein contains a P-loop motif that binds GTP and a highly conserved 17-residue targeting sequence responsible for its localization to the mitochondria.[5][7][8][9] Of interest, many of the phosphorylation sites on this protein are highly conserved and clustered around GTP-binding motifs.[5]

Several splice variants were observed in human ESTs that differ largely in the 5’ UTR region.[3][10] Pseudogenes for this gene are also found in chromosomes 1 and 2.[3]

Function

DAP3 is a 28S subunit protein of mitoribosomes and localizes to the mitochondrial matrix.[3][4][5] As part of the mitoribosome, DAP3 participates in the translation of the 13 ETC complex proteins encoded in the mitochondrial genome, and consequently, in the regulation of cellular respiration.[3][4][5][6] As a member of the death-associated protein (DAP) family, DAP3 can also be found outside of the mitochondria to initiate the extrinsic apoptotic pathway through its interactions with apoptotic factors, such as tumor necrosis factor-alpha, Fas ligand, and gamma interferon.[3][4][7][8][9] Additionally, DAP3 interacts with the factor IPS-1 to activate caspases 3, 8, and 9, resulting in a type of extracellular apoptosis called anoikis.[8][9] Moreover, DAP3 may contribute to apoptosis through its mediation of mitochondrial fragmentation, as this function extends to the mediation of the oxidative stress response, reactive oxygen species (ROS) production, and ultimately, mitochondrial homeostasis.[6][7][9] DAP3 is essential for life, and its deletion in embryos is lethal.[10] Nonetheless, DAP3 and its apoptotic activity can be inhibited by AKT phosphorylation.[8][9]

Clinical significance

As aforementioned, death associated protein 3 (DAP3) has regulatory roles in cell respiration and apoptosis. Both opposites and cell respiration are important elements of cell death pathways and have underlying mechanistic roles in ischemia-reperfusion injury.[11][12][13]

During a normal embryologic processes, or during cell injury (such as ischemia-reperfusion injury during heart attacks and strokes) or during developments and processes in cancer, an apoptotic cell undergoes structural changes including cell shrinkage, plasma membrane blebbing, nuclear condensation, and fragmentation of the DNA and nucleus. This is followed by fragmentation into apoptotic bodies that are quickly removed by phagocytes, thereby preventing an inflammatory response.[14] It is a mode of cell death defined by characteristic morphological, biochemical and molecular changes. It was first described as a "shrinkage necrosis", and then this term was replaced by apoptosis to emphasize its role opposite mitosis in tissue kinetics. In later stages of apoptosis the entire cell becomes fragmented, forming a number of plasma membrane-bounded apoptotic bodies which contain nuclear and or cytoplasmic elements. The ultrastructural appearance of necrosis is quite different, the main features being mitochondrial swelling, plasma membrane breakdown and cellular disintegration. Apoptosis occurs in many physiological and pathological processes. It plays an important role during embryonal development as programmed cell death and accompanies a variety of normal involutional processes in which it serves as a mechanism to remove "unwanted" cells.

DAP3 has been implicated in numerous cancers. Studies demonstrated that DAP3 expression tended to be low to nonexistent in the tumor cells of B-cell lymphoma, non-small cell lung cancer, head and neck cancer, breast cancer, gastric cancer, and colon cancer, possibly due to hypermethylation of the gene’s promoter.[7][8] Moreover, DAP3 expression has been positively correlated with improved cancer prognosis, indicating that the protein combats cancer progression through its proapoptotic function.[7][8] As a result, DAP3 could serve as a potential biomarker to monitor the effectiveness of therapeutic treatments such as chemotherapy.[7] However, in other cancers, such as glioblastoma multiforme (GBM) and thymoma, DAP3 expression was found to be upregulated.[6][10] Thus, the specific role of DAP3 in various cancers requires further study.[13]

Interactions

DAP3 has been shown to interact with:

References

  1. ↑ Kissil JL, Deiss LP, Bayewitch M, Raveh T, Khaspekov G, Kimchi A (Nov 1995). "Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death". The Journal of Biological Chemistry. 270 (46): 27932–6. doi:10.1074/jbc.270.46.27932. PMID 7499268.
  2. ↑ Kissil JL, Kimchi A (September 1997). "Assignment of death associated protein 3 (DAP3) to human chromosome 1q21 by in situ hybridization". Cytogenetics and Cell Genetics. 77 (3–4): 252. doi:10.1159/000134587. PMID 9284927.
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 "Entrez Gene: DAP3 death associated protein 3".
  4. ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Tang T, Zheng B, Chen SH, Murphy AN, Kudlicka K, Zhou H, Farquhar MG (Feb 2009). "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis". The Journal of Biological Chemistry. 284 (8): 5414–24. doi:10.1074/jbc.M807797200. PMC 2643507. PMID 19103604.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 Miller JL, Koc H, Koc EC (Feb 2008). "Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3". Protein Science. 17 (2): 251–60. doi:10.1110/ps.073185608. PMC 2222727. PMID 18227431.
  6. ↑ 6.0 6.1 6.2 6.3 6.4 Jacques C, Fontaine JF, Franc B, Mirebeau-Prunier D, Triau S, Savagner F, Malthiery Y (Jul 2009). "Death-associated protein 3 is overexpressed in human thyroid oncocytic tumours". British Journal of Cancer. 101 (1): 132–8. doi:10.1038/sj.bjc.6605111. PMC 2713694. PMID 19536094.
  7. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 Jia Y, Ye L, Ji K, Zhang L, Hargest R, Ji J, Jiang WG (Jan 2014). "Death-associated protein-3, DAP-3, correlates with preoperative chemotherapy effectiveness and prognosis of gastric cancer patients following perioperative chemotherapy and radical gastrectomy". British Journal of Cancer. 110 (2): 421–9. doi:10.1038/bjc.2013.712. PMC 3899757. PMID 24300973.
  8. ↑ 8.00 8.01 8.02 8.03 8.04 8.05 8.06 8.07 8.08 8.09 8.10 Wazir U, Jiang WG, Sharma AK, Mokbel K (Feb 2012). "The mRNA expression of DAP3 in human breast cancer: correlation with clinicopathological parameters". Anticancer Research. 32 (2): 671–4. PMID 22287761.
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 Miyazaki T, Shen M, Fujikura D, Tosa N, Kim HR, Kon S, Uede T, Reed JC (Oct 2004). "Functional role of death-associated protein 3 (DAP3) in anoikis". The Journal of Biological Chemistry. 279 (43): 44667–72. doi:10.1074/jbc.M408101200. PMID 15302871.
  10. ↑ 10.0 10.1 10.2 10.3 10.4 10.5 10.6 Han MJ, Chiu DT, Koc EC (Apr 2010). "Regulation of mitochondrial ribosomal protein S29 (MRPS29) expression by a 5'-upstream open reading frame". Mitochondrion. 10 (3): 274–83. doi:10.1016/j.mito.2009.12.150. PMC 2844934. PMID 20079882.
  11. ↑ Gracia-Sancho J, Casillas-Ramírez A, Peralta C (Aug 2015). "Molecular pathways in protecting the liver from ischaemia/reperfusion injury: a 2015 update". Clinical Science. 129 (4): 345–62. doi:10.1042/CS20150223. PMID 26014222.
  12. ↑ Ekert PG, Vaux DL (Dec 2005). "The mitochondrial death squad: hardened killers or innocent bystanders?". Current Opinion in Cell Biology. 17 (6): 626–30. doi:10.1016/j.ceb.2005.09.001. PMID 16219456.
  13. ↑ 13.0 13.1 Kissil JL, Kimchi A (Jun 1998). "Death-associated proteins: from gene identification to the analysis of their apoptotic and tumour suppressive functions". Molecular Medicine Today. 4 (6): 268–74. doi:10.1016/s1357-4310(98)01263-5. PMID 9679246.
  14. ↑ Kerr JF, Wyllie AH, Currie AR (Aug 1972). "Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics". British Journal of Cancer. 26 (4): 239–57. doi:10.1038/bjc.1972.33. PMC 2008650. PMID 4561027.
  15. ↑ 15.0 15.1 Miyazaki T, Reed JC (Jun 2001). "A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins". Nature Immunology. 2 (6): 493–500. doi:10.1038/88684. PMID 11376335.
  16. ↑ 16.0 16.1 Hulkko SM, Wakui H, Zilliacus J (Aug 2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function". The Biochemical Journal. 349 (3): 885–93. doi:10.1042/bj3490885. PMC 1221218. PMID 10903152.

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Hulkko SM, Wakui H, Zilliacus J (2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function". Biochem. J. 349 (Pt 3): 885–93. doi:10.1042/bj3490885. PMC 1221218. PMID 10903152.
  • Morgan CJ, Jacques C, Savagner F, Tourmen Y, Mirebeau DP, Malthièry Y, Reynier P (2001). "A conserved N-terminal sequence targets human DAP3 to mitochondria". Biochem. Biophys. Res. Commun. 280 (1): 177–81. doi:10.1006/bbrc.2000.4119. PMID 11162496.
  • Cavdar Koc E, Ranasinghe A, Burkhart W, Blackburn K, Koc H, Moseley A, Spremulli LL (2001). "A new face on apoptosis: death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins". FEBS Lett. 492 (1–2): 166–70. doi:10.1016/S0014-5793(01)02250-5. PMID 11248257.
  • Cavdar Koc E, Burkhart W, Blackburn K, Moseley A, Spremulli LL (2001). "The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present". J. Biol. Chem. 276 (22): 19363–74. doi:10.1074/jbc.M100727200. PMID 11279123.
  • Miyazaki T, Reed JC (2001). "A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins". Nat. Immunol. 2 (6): 493–500. doi:10.1038/88684. PMID 11376335.
  • Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K (2001). "Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit". J. Biol. Chem. 276 (35): 33181–95. doi:10.1074/jbc.M103236200. PMID 11402041.
  • Kenmochi N, Suzuki T, Uechi T, Magoori M, Kuniba M, Higa S, Watanabe K, Tanaka T (2001). "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders". Genomics. 77 (1–2): 65–70. doi:10.1006/geno.2001.6622. PMID 11543634.
  • Berger T, Kretzler M (2002). "Interaction of DAP3 and FADD only after cellular disruption". Nat. Immunol. 3 (1): 3–5. doi:10.1038/ni0102-3b. PMID 11753396.
  • Hulkko SM, Zilliacus J (2002). "Functional interaction between the pro-apoptotic DAP3 and the glucocorticoid receptor". Biochem. Biophys. Res. Commun. 295 (3): 749–55. doi:10.1016/S0006-291X(02)00713-1. PMID 12099703.
  • Berger T, Kretzler M (2002). "TRAIL-induced apoptosis is independent of the mitochondrial apoptosis mediator DAP3". Biochem. Biophys. Res. Commun. 297 (4): 880–4. doi:10.1016/S0006-291X(02)02310-0. PMID 12359235.
  • Zhang Z, Gerstein M (2003). "Identification and characterization of over 100 mitochondrial ribosomal protein pseudogenes in the human genome". Genomics. 81 (5): 468–80. doi:10.1016/S0888-7543(03)00004-1. PMID 12706105.
  • Mukamel Z, Kimchi A (2004). "Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death". J. Biol. Chem. 279 (35): 36732–8. doi:10.1074/jbc.M400041200. PMID 15175341.
  • Hirota T, Obara K, Matsuda A, Akahoshi M, Nakashima K, Hasegawa K, Takahashi N, Shimizu M, Sekiguchi H, Kokubo M, Doi S, Fujiwara H, Miyatake A, Fujita K, Enomoto T, Kishi F, Suzuki Y, Saito H, Nakamura Y, Shirakawa T, Tamari M (2004). "Association between genetic variation in the gene for death-associated protein-3 (DAP3) and adult asthma". J. Hum. Genet. 49 (7): 370–5. doi:10.1007/s10038-004-0161-4. PMID 15179560.
  • Miyazaki T, Shen M, Fujikura D, Tosa N, Kim HR, Kon S, Uede T, Reed JC (2004). "Functional role of death-associated protein 3 (DAP3) in anoikis". J. Biol. Chem. 279 (43): 44667–72. doi:10.1074/jbc.M408101200. PMID 15302871.
  • Sasaki H, Ide N, Yukiue H, Kobayashi Y, Fukai I, Yamakawa Y, Fujii Y (2004). "Arg and DAP3 expression was correlated with human thymoma stage". Clin. Exp. Metastasis. 21 (6): 507–13. doi:10.1007/s10585-004-2153-3. PMID 15679048.
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