BCL2L2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Bcl-2-like protein 2''' is a [[protein]] that in humans is encoded by the ''BCL2L2'' [[gene]].<ref name="pmid8761287">{{cite journal | vauthors = Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S | title = bcl-w, a novel member of the bcl-2 family, promotes cell survival | journal = Oncogene | volume = 13 | issue = 4 | pages = 665–75 |date=October 1996 | pmid = 8761287 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BCL2L2 BCL2-like 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=599| accessdate = }}</ref> It was originally discovered by Leonie Gibson, [[Suzanne Cory]] and colleagues at the [[Walter and Eliza Hall Institute of Medical Research]], who called it '''Bcl-w'''.<ref name="Gibson1996">{{cite journal  | vauthors=Gibson L, Holmgreen SP, Huang DC |title=bcl-w, a novel member of the bcl-2 family, promotes cell survival. |journal=Oncogene |volume=13 |issue= 4 |pages= 665–75 |year= 1996 |pmid= 8761287 |doi= |display-authors=etal}}</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. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_BCL2L2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mk3.
| PDB = {{PDB2|1mk3}}, {{PDB2|1o0l}}, {{PDB2|1zy3}}
| Name = BCL2-like 2
| HGNCid = 995
| Symbol = BCL2L2
| AltSymbols =; BCL-W; BCLW; KIAA0271
| OMIM = 601931
| ECnumber = 
| Homologene = 2989
| MGIid = 108052
| GeneAtlas_image1 = PBB_GE_BCL2L2_209311_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 599
    | Hs_Ensembl = ENSG00000129473
    | Hs_RefseqProtein = NP_004041
    | Hs_RefseqmRNA = NM_004050
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 22845866
    | Hs_GenLoc_end = 22850798
    | Hs_Uniprot = Q92843
    | Mm_EntrezGene = 12050
    | Mm_Ensembl = ENSMUSG00000022194
    | Mm_RefseqmRNA = NM_007537
    | Mm_RefseqProtein = NP_031563
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 53837600
    | Mm_GenLoc_end = 53842435
    | Mm_Uniprot = P70345
  }}
}}
'''BCL2-like 2''', also known as '''BCL2L2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCL2L2 BCL2-like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=599| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a pro-survival (anti-[[apoptosis|apoptotic]]) member of the [[bcl-2]] [[protein]] family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under [[cytotoxicity|cytotoxic]] conditions. Studies of the related gene in mice indicated a role in the survival of [[Nerve growth factor|NGF]]- and [[BDNF]]-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult [[spermatogenesis]].<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
Relative to its [[Bcl-2]] counterparts there is considerably less data on this particular protein. Located on chromosome 14q11 it appears to be redundant in most tissues apart from specific examples.
| summary_text = This gene encodes a member of the BCL-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.<ref name="entrez">{{cite web | title = Entrez Gene: BCL2L2 BCL2-like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=599| accessdate = }}</ref>
 
}}
==Interactions==
BCL2L2 has been shown to [[Protein-protein interaction|interact]] with:
* [[BCL2L11]]<ref name="pmid9731710">{{cite journal | vauthors = Hsu SY, Lin P, Hsueh AJ | title = BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members | journal = Mol. Endocrinol. | volume = 12 | issue = 9 | pages = 1432–40 |date=September 1998  | pmid = 9731710 | doi = 10.1210/mend.12.9.0166 }}</ref><ref name = pmid9430630>{{cite journal | date = January 1998 | vauthors = O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC | title = Bim: a novel member of the Bcl-2 family that promotes apoptosis | journal = EMBO J. | volume = 17 | issue = 2 | pages = 384–95  | pmid = 9430630 | pmc = 1170389 | doi = 10.1093/emboj/17.2.384}}</ref>
* [[Bcl-2-associated death promoter|BAD]],<ref name = pmid12115603/><ref name = pmid15694340>{{cite journal | date = February 2005 | vauthors = Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC | title = Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | journal = Mol. Cell | volume = 17 | issue = 3 | pages = 393–403  | pmid = 15694340 | doi = 10.1016/j.molcel.2004.12.030}}</ref><ref name = pmid11483855>{{cite journal | date = October 2001 | vauthors = Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ | title = Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis | journal = Apoptosis | volume = 6 | issue = 5 | pages = 319–30  | pmid = 11483855 | doi = 10.1023/A:1011319901057}}</ref><ref name = pmid10381646>{{cite journal | date = June 1999 | vauthors = Holmgreen SP, Huang DC, Adams JM, Cory S | title = Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members | journal = Cell Death Differ. | volume = 6 | issue = 6 | pages = 525–32  | pmid = 10381646 | doi = 10.1038/sj.cdd.4400519}}</ref> and
* [[PPP1CA]].<ref name = pmid12115603>{{cite journal | date = July 2002 | vauthors = Ayllón V, Cayla X, García A, Fleischer A, Rebollo A | title = The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad | journal = Eur. J. Immunol. | volume = 32 | issue = 7 | pages = 1847–55  | pmid = 12115603 | doi = 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7}}</ref>


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Nagase T, Seki N, Ishikawa K |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321–9, 341–54 |year= 1997 |pmid= 9039502 |doi=10.1093/dnares/3.5.321  |display-authors=etal}}
| citations =
*{{cite journal | vauthors=O'Connor L, Strasser A, O'Reilly LA |title=Bim: a novel member of the Bcl-2 family that promotes apoptosis. |journal=EMBO J. |volume=17 |issue= 2 |pages= 384–95 |year= 1998 |pmid= 9430630 |doi= 10.1093/emboj/17.2.384 | pmc=1170389 |display-authors=etal}}
*{{cite journal  | author=Gibson L, Holmgreen SP, Huang DC, ''et al.'' |title=bcl-w, a novel member of the bcl-2 family, promotes cell survival. |journal=Oncogene |volume=13 |issue= 4 |pages= 665-75 |year= 1996 |pmid= 8761287 |doi= }}
*{{cite journal  | vauthors=Ross AJ, Waymire KG, Moss JE |title=Testicular degeneration in Bclw-deficient mice. |journal=Nat. Genet. |volume=18 |issue= 3 |pages= 251–6 |year= 1998 |pmid= 9500547 |doi= 10.1038/ng0398-251 |display-authors=etal}}
*{{cite journal  | author=Nagase T, Seki N, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321-9, 341-54 |year= 1997 |pmid= 9039502 |doi=  }}
*{{cite journal  | vauthors=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432–40 |year= 1998 |pmid= 9731710 |doi=10.1210/mend.12.9.0166  }}
*{{cite journal  | author=O'Connor L, Strasser A, O'Reilly LA, ''et al.'' |title=Bim: a novel member of the Bcl-2 family that promotes apoptosis. |journal=EMBO J. |volume=17 |issue= 2 |pages= 384-95 |year= 1998 |pmid= 9430630 |doi= 10.1093/emboj/17.2.384 }}
*{{cite journal  | vauthors=Middleton G, Wyatt S, Ninkina N, Davies AM |title=Reciprocal developmental changes in the roles of Bcl-w and Bcl-x(L) in regulating sensory neuron survival. |journal=Development |volume=128 |issue= 3 |pages= 447–57 |year= 2001 |pmid= 11152643 |doi=  }}
*{{cite journal  | author=Ross AJ, Waymire KG, Moss JE, ''et al.'' |title=Testicular degeneration in Bclw-deficient mice. |journal=Nat. Genet. |volume=18 |issue= 3 |pages= 251-6 |year= 1998 |pmid= 9500547 |doi= 10.1038/ng0398-251 }}
*{{cite journal  | vauthors=O'Reilly LA, Print C, Hausmann G |title=Tissue expression and subcellular localization of the pro-survival molecule Bcl-w. |journal=Cell Death Differ. |volume=8 |issue= 5 |pages= 486–94 |year= 2001 |pmid= 11423909 |doi= 10.1038/sj.cdd.4400835 |display-authors=etal}}
*{{cite journal  | author=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432-40 |year= 1998 |pmid= 9731710 |doi=  }}
*{{cite journal  | vauthors=Bae J, Hsu SY, Leo CP |title=Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis. |journal=Apoptosis |volume=6 |issue= 5 |pages= 319–30 |year= 2001 |pmid= 11483855 |doi=10.1023/A:1011319901057  |display-authors=etal}}
*{{cite journal  | author=Middleton G, Wyatt S, Ninkina N, Davies AM |title=Reciprocal developmental changes in the roles of Bcl-w and Bcl-x(L) in regulating sensory neuron survival. |journal=Development |volume=128 |issue= 3 |pages= 447-57 |year= 2001 |pmid= 11152643 |doi= }}
*{{cite journal  | vauthors=Puthalakath H, Villunger A, O'Reilly LA |title=Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. |journal=Science |volume=293 |issue= 5536 |pages= 1829–32 |year= 2001 |pmid= 11546872 |doi= 10.1126/science.1062257 |display-authors=etal}}
*{{cite journal  | author=O'Reilly LA, Print C, Hausmann G, ''et al.'' |title=Tissue expression and subcellular localization of the pro-survival molecule Bcl-w. |journal=Cell Death Differ. |volume=8 |issue= 5 |pages= 486-94 |year= 2001 |pmid= 11423909 |doi= 10.1038/sj/cdd/4400835 }}
*{{cite journal  | vauthors=Ayllón V, Cayla X, García A |title=The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad. |journal=Eur. J. Immunol. |volume=32 |issue= 7 |pages= 1847–55 |year= 2002 |pmid= 12115603 |doi= 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7 |display-authors=etal}}
*{{cite journal  | author=Bae J, Hsu SY, Leo CP, ''et al.'' |title=Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis. |journal=Apoptosis |volume=6 |issue= 5 |pages= 319-30 |year= 2001 |pmid= 11483855 |doi= }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Puthalakath H, Villunger A, O'Reilly LA, ''et al.'' |title=Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. |journal=Science |volume=293 |issue= 5536 |pages= 1829-32 |year= 2001 |pmid= 11546872 |doi= 10.1126/science.1062257 }}
*{{cite journal  | vauthors=Denisov AY, Madiraju MS, Chen G |title=Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix. |journal=J. Biol. Chem. |volume=278 |issue= 23 |pages= 21124–8 |year= 2003 |pmid= 12651847 |doi= 10.1074/jbc.M301798200 |display-authors=etal}}
*{{cite journal  | author=Ayllón V, Cayla X, García A, ''et al.'' |title=The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad. |journal=Eur. J. Immunol. |volume=32 |issue= 7 |pages= 1847-55 |year= 2002 |pmid= 12115603 |doi= 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7 }}
*{{cite journal  | vauthors=Hinds MG, Lackmann M, Skea GL |title=The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. |journal=EMBO J. |volume=22 |issue= 7 |pages= 1497–507 |year= 2003 |pmid= 12660157 |doi= 10.1093/emboj/cdg144  | pmc=152889 |display-authors=etal}}
*{{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=Wilson-Annan J, O'Reilly LA, Crawford SA |title=Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity. |journal=J. Cell Biol. |volume=162 |issue= 5 |pages= 877–87 |year= 2003 |pmid= 12952938 |doi= 10.1083/jcb.200302144  | pmc=2172834 |display-authors=etal}}
*{{cite journal  | author=Denisov AY, Madiraju MS, Chen G, ''et al.'' |title=Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix. |journal=J. Biol. Chem. |volume=278 |issue= 23 |pages= 21124-8 |year= 2003 |pmid= 12651847 |doi= 10.1074/jbc.M301798200 }}
*{{cite journal  | vauthors=Zhu X, Wang Y, Ogawa O |title=Neuroprotective properties of Bcl-w in Alzheimer disease. |journal=J. Neurochem. |volume=89 |issue= 5 |pages= 1233–40 |year= 2004 |pmid= 15147516 |doi= 10.1111/j.1471-4159.2004.02416.x |display-authors=etal}}
*{{cite journal  | author=Hinds MG, Lackmann M, Skea GL, ''et al.'' |title=The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. |journal=EMBO J. |volume=22 |issue= 7 |pages= 1497-507 |year= 2003 |pmid= 12660157 |doi= 10.1093/emboj/cdg144 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Wilson-Annan J, O'Reilly LA, Crawford SA, ''et al.'' |title=Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity. |journal=J. Cell Biol. |volume=162 |issue= 5 |pages= 877-87 |year= 2003 |pmid= 12952938 |doi= 10.1083/jcb.200302144 }}
*{{cite journal  | vauthors=Chen L, Willis SN, Wei A |title=Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 393–403 |year= 2005 |pmid= 15694340 |doi= 10.1016/j.molcel.2004.12.030 |display-authors=etal}}
*{{cite journal  | author=Zhu X, Wang Y, Ogawa O, ''et al.'' |title=Neuroprotective properties of Bcl-w in Alzheimer disease. |journal=J. Neurochem. |volume=89 |issue= 5 |pages= 1233-40 |year= 2004 |pmid= 15147516 |doi= 10.1111/j.1471-4159.2004.02416.x }}
*{{cite journal  | vauthors=Kimura K, Wakamatsu A, Suzuki Y |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Denisov AY, Chen G, Sprules T |title=Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles. |journal=Biochemistry |volume=45 |issue= 7 |pages= 2250–6 |year= 2006 |pmid= 16475813 |doi= 10.1021/bi052332s |display-authors=etal}}
*{{cite journal  | author=Chen L, Willis SN, Wei A, ''et al.'' |title=Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 393-403 |year= 2005 |pmid= 15694340 |doi= 10.1016/j.molcel.2004.12.030 }}
*{{cite journal  | vauthors=Certo M, Del Gaizo Moore V, Nishino M |title=Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. |journal=Cancer Cell |volume=9 |issue= 5 |pages= 351–65 |year= 2006 |pmid= 16697956 |doi= 10.1016/j.ccr.2006.03.027 |display-authors=etal}}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
{{Refend}}
*{{cite journal  | author=Denisov AY, Chen G, Sprules T, ''et al.'' |title=Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles. |journal=Biochemistry |volume=45 |issue= 7 |pages= 2250-6 |year= 2006 |pmid= 16475813 |doi= 10.1021/bi052332s }}
==External links==
*{{cite journal  | author=Certo M, Del Gaizo Moore V, Nishino M, ''et al.'' |title=Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. |journal=Cancer Cell |volume=9 |issue= 5 |pages= 351-65 |year= 2006 |pmid= 16697956 |doi= 10.1016/j.ccr.2006.03.027 }}
* {{UCSC gene info|BCL2L2}}
}}
{{PDB Gallery|geneid=599}}
{{refend}}
 


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{{Gene-14-stub}}
{{WikiDoc Sources}}

Latest revision as of 02:32, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Bcl-2-like protein 2 is a protein that in humans is encoded by the BCL2L2 gene.[1][2] It was originally discovered by Leonie Gibson, Suzanne Cory and colleagues at the Walter and Eliza Hall Institute of Medical Research, who called it Bcl-w.[3]

Function

This gene encodes a pro-survival (anti-apoptotic) member of the bcl-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.[2]

Relative to its Bcl-2 counterparts there is considerably less data on this particular protein. Located on chromosome 14q11 it appears to be redundant in most tissues apart from specific examples.

Interactions

BCL2L2 has been shown to interact with:

References

  1. ↑ Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S (October 1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.
  2. ↑ 2.0 2.1 "Entrez Gene: BCL2L2 BCL2-like 2".
  3. ↑ Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.
  4. ↑ Hsu SY, Lin P, Hsueh AJ (September 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members". Mol. Endocrinol. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.
  5. ↑ O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (January 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
  6. ↑ 6.0 6.1 Ayllón V, Cayla X, García A, Fleischer A, Rebollo A (July 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.
  7. ↑ Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
  8. ↑ Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (October 2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30. doi:10.1023/A:1011319901057. PMID 11483855.
  9. ↑ Holmgreen SP, Huang DC, Adams JM, Cory S (June 1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID 10381646.

Further reading

External links


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