THOC5: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (→‎top: task, replaced: EMBO journal → EMBO Journal using AWB)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Underlinked|date=June 2016}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''THO complex subunit 5 homolog''' is a [[protein]] that in humans is encoded by the ''THOC5'' [[gene]].[http://www.biosignaling.com/content/12/1/3 THOC5] is a member of THO complex which is a subcomplex of the transcription/export complex (TREX). THOC5 is evolutionarily conserved in higher eukaryotes, however the exact roles of THOC5 in transcription and mRNA export are still unclear. THOC5 is phosphorylated by several protein kinases at multiple residues upon extracellular stimuli. These include stimulation with growth factors/cytokines/chemokines, or DNA damage reagents. Furthermore, THOC5 is a substrate for several oncogenic tyrosine kinases, suggesting that THOC5 may be involved in cancer development. Recent THOC5 knockout mouse data reveal that THOC5 is an essential element in the maintenance of stem cells and growth factor/cytokine-mediated differentiation/proliferation. Furthermore, depletion of THOC5 influences less than 1% of total mRNA export in the steady state, however it influences more than 90% of growth factor/cytokine induced genes. THOC5, thereby contributes to the 3′ processing and/or export of immediate-early genes induced by extracellular stimuli. These studies bring new insight into the link between the mRNA export complex and immediate-early gene response. The data from these studies also suggest that THOC5 may be a useful tool for studying stem cell biology, for modifying the differentiation processes and for cancer therapy.<ref>Tran DDH, Koch A and Tamura T. THOC5, a member of the mRNA export complex: a novel link between mRNA export machinery and signal transduction pathways in cell proliferation and differentiation. Cell Communication and Signaling 2014, 12:3</ref><ref>Tran DD, Saran S, Dittrich-Breiholz O, Williamson AJ, Klebba-Farber S, Koch A, Kracht M, Whetton AD, Tamura T (2013) Transcriptional regulation of immediate-early gene response by THOC5, a member of mRNA export complex, contributes to the M-CSF-induced macrophage differentiation. Cell death & disease 4: e879</ref><ref>Saran S, Tran DD, Klebba-Farber S, Moran-Losada P, Wiehlmann L, Koch A, Chopra H, Pabst O, Hoffmann A, Klopfleisch R, Tamura T (2013) THOC5, a member of the mRNA export complex, contributes to processing of a subset of wingless/integrated (Wnt) target mRNAs and integrity of the gut epithelial barrier. BMC Cell Biol 14: 51</ref><ref>Griaud, F., Pierce, A., Gonzalez Sanchez, M.B., Scott, M., Abraham, S.A., Holyoake, T.L., Tran, D.D., Tamura, T., and Whetton, A.D. (2013). A pathway from leukemogenic oncogenes and stem cell chemokines to RNA processing via THOC5. Leukemia 27, 932-940.</ref><ref>Katahira J, Okuzaki D, Inoue H, Yoneda Y, Maehara K, Ohkawa Y (2013) Human TREX component Thoc5 affects alternative polyadenylation site choice by recruiting mammalian cleavage factor I. Nucleic Acids Research 41: 7060-7072</ref><ref>Katahira J, Inoue H, Hurt E, Yoneda Y (2009) Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA. The EMBO Journal 28: 556-567</ref><ref>Ramachandran S., Tran DD., Klebba-Faerber S., Kardinal C., Whetton AD., Tamura T. An ataxia-teleaniectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5. RNA 17(11):1957-66, 2011</ref><ref>Guria A., Tran D.D.H,Ramachandran S.,Koch A.,Bounkari O.,Dutta P,Hauser H,Tamura  T. Identification of mRNAs that are spliced but not exported to the cytoplasm in the absence of THOC5 in mouse embryo fibroblasts, RNA, 2011 17:00-00.</ref><ref>Mancini,  A.,  Niemann-Seyde, S. C., Pankow, R.,  El Bounkari, O., Klebba-Färber, S., Koch, A., EJaworska, E., Spooncer, E., Gruber, A. D. , Whetton, A. D., Tamura, T. (2010) THOC5/FMIP, an mRNA export TREX complex protein, is essential for hematopoietic primitive cell survival in vivo. BMC Biology 8, 1.</ref><ref>Mancini, A., El Bounkari, O., Norrenbrock, A-F., Scherr, M., Schaefer, D., Eder M., Banham, A. H., Pulford, K., Lyne, L., Whetton A. D., and Tamura, T. (2007) FMIP controls the adipocyte lineage commitment of C2C12 cells by down-modulation of C/EBPalpha. Oncogene 26, 1020-1027.</ref><ref>Mancini A., Koch A., Whetton A.D., and Tamura T. (2004)The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation and thereby potentiates M-CSF-mediated differentiation. Oncogene, 23, 6581-9.</ref><ref>Tamura,  T.,  Mancini, A., Joos,  H., Koch, A.,  Hakim,  C.,  Dumanski, J., Weidner, K.M.,  and Niemann, H. (1999) FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage. Oncogene, 18, 6488-6495.</ref>
| 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. -->
<ref name="pmid11979277">{{cite journal | vauthors = Strasser K, Masuda S, Mason P, Pfannstiel J, Oppizzi M, Rodriguez-Navarro S, Rondon AG, Aguilera A, Struhl K, Reed R, Hurt E | title = TREX is a conserved complex coupling transcription with messenger RNA export | journal = Nature | volume = 417 | issue = 6886 | pages = 304–8 |date=May 2002 | pmid = 11979277 | pmc = | doi = 10.1038/nature746 }}</ref><ref name="pmid8242058">{{cite journal | vauthors = Xie YG, Han FY, Peyrard M, Ruttledge MH, Fransson I, DeJong P, Collins J, Dunham I, Nordenskjold M, Dumanski JP | title = Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid contig in the neurofibromatosis type 2/meningioma region on human chromosome 22q12 | journal = Hum Mol Genet | volume = 2 | issue = 9 | pages = 1361–8 |date=Dec 1993 | pmid = 8242058 | pmc =  | doi =10.1093/hmg/2.9.1361 }}</ref><ref name="pmid10231032">{{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 6 | issue = 1 | pages = 63–70 |date=Jul 1999 | pmid = 10231032 | pmc = | doi =10.1093/dnares/6.1.63  }}</ref><ref name="pmid19015024">{{cite journal | vauthors = Carney L, Pierce A, Rijnen M, Gonzalez Sanchez MB, Hamzah HG, Zhang L, Tamura T, Whetton AD | title = THOC5 couples M-CSF receptor signaling to transcription factor expression | journal = Cell Signal | volume = 21 | issue = 2 | pages = 309–16 |date=Dec 2008 | pmid = 19015024 | pmc = | doi = 10.1016/j.cellsig.2008.10.018 }}</ref><ref name="pmid18373705">{{cite journal | vauthors = Pierce A, Carney L, Hamza HG, Griffiths JR, Zhang L, Whetton BA, Gonzalez Sanchez MB, Tamura T, Sternberg D, Whetton AD | title = THOC5 spliceosome protein: a target for leukaemogenic tyrosine kinases that affects inositol lipid turnover | journal = Br J Haematol | volume = 141 | issue = 5 | pages = 641–50 |date=May 2008 | pmid = 18373705 | pmc =  | doi = 10.1111/j.1365-2141.2008.07090.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: THOC5 THO complex 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8563| accessdate = }}</ref>
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = THO complex 5
| HGNCid = 19074
| Symbol = THOC5
| AltSymbols =; C22orf19; Fmip; PK1.3
| OMIM =
| ECnumber =
  | Homologene = 37836
  | MGIid = 1351333
| GeneAtlas_image1 = PBB_GE_THOC5_209418_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_THOC5_209419_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component =  
| Process = {{GNF_GO|id=GO:0045650 |text = negative regulation of macrophage differentiation}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8563
    | Hs_Ensembl = ENSG00000100296
    | Hs_RefseqProtein = NP_001002877
    | Hs_RefseqmRNA = NM_001002877
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 28231868
    | Hs_GenLoc_end = 28279703
    | Hs_Uniprot = Q13769
    | Mm_EntrezGene = 107829
    | Mm_Ensembl = ENSMUSG00000034274
    | Mm_RefseqmRNA = NM_172438
    | Mm_RefseqProtein = NP_766026
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 4795346
    | Mm_GenLoc_end = 4828868
    | Mm_Uniprot =   
  }}
}}
'''THO complex 5''', also known as '''THOC5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: THOC5 THO complex 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8563| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Line 56: Line 12:


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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=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  }}
*{{cite journal  | author=Xie YG, Han FY, Peyrard M, ''et al.'' |title=Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid contig in the neurofibromatosis type 2/meningioma region on human chromosome 22q12. |journal=Hum. Mol. Genet. |volume=2 |issue= 9 |pages= 1361-8 |year= 1993 |pmid= 8242058 |doi= }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |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=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=Tamura T, Mancini A, Joos H, etal |title=FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage differentiation |journal=Oncogene |volume=18 |issue= 47 |pages= 6488–95 |year= 2000 |pmid= 10597251 |doi= 10.1038/sj.onc.1203062 }}
*{{cite journal  | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63-70 |year= 1999 |pmid= 10231032 |doi= }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{cite journal | author=Tamura T, Mancini A, Joos H, ''et al.'' |title=FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage differentiation. |journal=Oncogene |volume=18 |issue= 47 |pages= 6488-95 |year= 2000 |pmid= 10597251 |doi= 10.1038/sj.onc.1203062 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Strässer K, Masuda S, Mason P, ''et al.'' |title=TREX is a conserved complex coupling transcription with messenger RNA export. |journal=Nature |volume=417 |issue= 6886 |pages= 304-8 |year= 2002 |pmid= 11979277 |doi= 10.1038/417304a }}
*{{cite journal  | vauthors=Mancini A, Koch A, Whetton AD, Tamura T |title=The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation |journal=Oncogene |volume=23 |issue= 39 |pages= 6581–9 |year= 2004 |pmid= 15221008 |doi= 10.1038/sj.onc.1207841 }}
*{{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=Collins JE, Wright CL, Edwards CA, etal |title=A genome annotation-driven approach to cloning the human ORFeome |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 | pmc=545604 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
*{{cite journal  | author=Mancini A, Koch A, Whetton AD, Tamura T |title=The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation. |journal=Oncogene |volume=23 |issue= 39 |pages= 6581-9 |year= 2004 |pmid= 15221008 |doi= 10.1038/sj.onc.1207841 }}
*{{cite journal   |vauthors=Carroll JS, Liu XS, Brodsky AS, etal |title=Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1 |journal=Cell |volume=122 |issue= 1 |pages= 33–43 |year= 2005 |pmid= 16009131 |doi= 10.1016/j.cell.2005.05.008 }}
*{{cite journal | author=Collins JE, Wright CL, Edwards CA, ''et al.'' |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 }}
*{{cite journal   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{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 | author=Carroll JS, Liu XS, Brodsky AS, ''et al.'' |title=Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1. |journal=Cell |volume=122 |issue= 1 |pages= 33-43 |year= 2005 |pmid= 16009131 |doi= 10.1016/j.cell.2005.05.008 }}
*{{cite journal | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
}}
}}
{{refend}}
{{refend}}


{{gene-22-stub}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{WikiDoc Sources}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

Latest revision as of 00:42, 31 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

THO complex subunit 5 homolog is a protein that in humans is encoded by the THOC5 gene.THOC5 is a member of THO complex which is a subcomplex of the transcription/export complex (TREX). THOC5 is evolutionarily conserved in higher eukaryotes, however the exact roles of THOC5 in transcription and mRNA export are still unclear. THOC5 is phosphorylated by several protein kinases at multiple residues upon extracellular stimuli. These include stimulation with growth factors/cytokines/chemokines, or DNA damage reagents. Furthermore, THOC5 is a substrate for several oncogenic tyrosine kinases, suggesting that THOC5 may be involved in cancer development. Recent THOC5 knockout mouse data reveal that THOC5 is an essential element in the maintenance of stem cells and growth factor/cytokine-mediated differentiation/proliferation. Furthermore, depletion of THOC5 influences less than 1% of total mRNA export in the steady state, however it influences more than 90% of growth factor/cytokine induced genes. THOC5, thereby contributes to the 3′ processing and/or export of immediate-early genes induced by extracellular stimuli. These studies bring new insight into the link between the mRNA export complex and immediate-early gene response. The data from these studies also suggest that THOC5 may be a useful tool for studying stem cell biology, for modifying the differentiation processes and for cancer therapy.[1][2][3][4][5][6][7][8][9][10][11][12]

[13][14][15][16][17][18]


References

  1. ↑ Tran DDH, Koch A and Tamura T. THOC5, a member of the mRNA export complex: a novel link between mRNA export machinery and signal transduction pathways in cell proliferation and differentiation. Cell Communication and Signaling 2014, 12:3
  2. ↑ Tran DD, Saran S, Dittrich-Breiholz O, Williamson AJ, Klebba-Farber S, Koch A, Kracht M, Whetton AD, Tamura T (2013) Transcriptional regulation of immediate-early gene response by THOC5, a member of mRNA export complex, contributes to the M-CSF-induced macrophage differentiation. Cell death & disease 4: e879
  3. ↑ Saran S, Tran DD, Klebba-Farber S, Moran-Losada P, Wiehlmann L, Koch A, Chopra H, Pabst O, Hoffmann A, Klopfleisch R, Tamura T (2013) THOC5, a member of the mRNA export complex, contributes to processing of a subset of wingless/integrated (Wnt) target mRNAs and integrity of the gut epithelial barrier. BMC Cell Biol 14: 51
  4. ↑ Griaud, F., Pierce, A., Gonzalez Sanchez, M.B., Scott, M., Abraham, S.A., Holyoake, T.L., Tran, D.D., Tamura, T., and Whetton, A.D. (2013). A pathway from leukemogenic oncogenes and stem cell chemokines to RNA processing via THOC5. Leukemia 27, 932-940.
  5. ↑ Katahira J, Okuzaki D, Inoue H, Yoneda Y, Maehara K, Ohkawa Y (2013) Human TREX component Thoc5 affects alternative polyadenylation site choice by recruiting mammalian cleavage factor I. Nucleic Acids Research 41: 7060-7072
  6. ↑ Katahira J, Inoue H, Hurt E, Yoneda Y (2009) Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA. The EMBO Journal 28: 556-567
  7. ↑ Ramachandran S., Tran DD., Klebba-Faerber S., Kardinal C., Whetton AD., Tamura T. An ataxia-teleaniectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5. RNA 17(11):1957-66, 2011
  8. ↑ Guria A., Tran D.D.H,Ramachandran S.,Koch A.,Bounkari O.,Dutta P,Hauser H,Tamura T. Identification of mRNAs that are spliced but not exported to the cytoplasm in the absence of THOC5 in mouse embryo fibroblasts, RNA, 2011 17:00-00.
  9. ↑ Mancini, A., Niemann-Seyde, S. C., Pankow, R., El Bounkari, O., Klebba-Färber, S., Koch, A., EJaworska, E., Spooncer, E., Gruber, A. D. , Whetton, A. D., Tamura, T. (2010) THOC5/FMIP, an mRNA export TREX complex protein, is essential for hematopoietic primitive cell survival in vivo. BMC Biology 8, 1.
  10. ↑ Mancini, A., El Bounkari, O., Norrenbrock, A-F., Scherr, M., Schaefer, D., Eder M., Banham, A. H., Pulford, K., Lyne, L., Whetton A. D., and Tamura, T. (2007) FMIP controls the adipocyte lineage commitment of C2C12 cells by down-modulation of C/EBPalpha. Oncogene 26, 1020-1027.
  11. ↑ Mancini A., Koch A., Whetton A.D., and Tamura T. (2004)The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation and thereby potentiates M-CSF-mediated differentiation. Oncogene, 23, 6581-9.
  12. ↑ Tamura, T., Mancini, A., Joos, H., Koch, A., Hakim, C., Dumanski, J., Weidner, K.M., and Niemann, H. (1999) FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage. Oncogene, 18, 6488-6495.
  13. ↑ Strasser K, Masuda S, Mason P, Pfannstiel J, Oppizzi M, Rodriguez-Navarro S, Rondon AG, Aguilera A, Struhl K, Reed R, Hurt E (May 2002). "TREX is a conserved complex coupling transcription with messenger RNA export". Nature. 417 (6886): 304–8. doi:10.1038/nature746. PMID 11979277.
  14. ↑ Xie YG, Han FY, Peyrard M, Ruttledge MH, Fransson I, DeJong P, Collins J, Dunham I, Nordenskjold M, Dumanski JP (Dec 1993). "Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid contig in the neurofibromatosis type 2/meningioma region on human chromosome 22q12". Hum Mol Genet. 2 (9): 1361–8. doi:10.1093/hmg/2.9.1361. PMID 8242058.
  15. ↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jul 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  16. ↑ Carney L, Pierce A, Rijnen M, Gonzalez Sanchez MB, Hamzah HG, Zhang L, Tamura T, Whetton AD (Dec 2008). "THOC5 couples M-CSF receptor signaling to transcription factor expression". Cell Signal. 21 (2): 309–16. doi:10.1016/j.cellsig.2008.10.018. PMID 19015024.
  17. ↑ Pierce A, Carney L, Hamza HG, Griffiths JR, Zhang L, Whetton BA, Gonzalez Sanchez MB, Tamura T, Sternberg D, Whetton AD (May 2008). "THOC5 spliceosome protein: a target for leukaemogenic tyrosine kinases that affects inositol lipid turnover". Br J Haematol. 141 (5): 641–50. doi:10.1111/j.1365-2141.2008.07090.x. PMID 18373705.
  18. ↑ "Entrez Gene: THOC5 THO complex 5".

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=THOC5&oldid=1420083"