ITGA9: Difference between revisions
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{{ | '''Integrin alpha-9''' is a [[protein]] that in humans is encoded by the ''ITGA9'' [[gene]].<ref name="pmid8245132">{{cite journal |vauthors=Palmer EL, Rüegg C, Ferrando R, Pytela R, Sheppard D | title = Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle | journal = J Cell Biol | volume = 123 | issue = 5 | pages = 1289–97 | date = Jan 1994 | pmid = 8245132 | pmc = 2119880 | doi = 10.1083/jcb.123.5.1289 }}</ref><ref name="pmid8290272">{{cite journal |vauthors=Hibi K, Yamakawa K, Ueda R, Horio Y, Murata Y, Tamari M, Uchida K, Takahashi T, Nakamura Y, Takahashi T | title = Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer | journal = Oncogene | volume = 9 | issue = 2 | pages = 611–9 | date = Feb 1994 | pmid = 8290272 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ITGA9 integrin, alpha 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3680| accessdate = }}</ref> | ||
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== Function == | |||
This gene encodes an alpha [[integrin]]. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for tenascin-C, VCAM1 and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.<ref name="entrez"/> | |||
==Interactions== | |||
The α9 subunit forms a heterodimeric complex with a β1 subunit to form the α9β1 integrin. This integrin participates in cell adhesion with various ligands in the extracellular matrix (ECM), including extra domain A (EDA) [[fibronectin]], [[Tenascin C|tenascin-C]], [[ADAM Protein|ADAMs]], EMELIN1, [[osteopontin]], and [[VEGF]].<ref>{{cite journal |vauthors=Høye AM, Couchman JR, Wewer UM, Fukami K, Yoneda A | title = The newcomer in the integrin family: integrin α9 in biology and cancer. | journal = Advances in biological regulation | volume = 52 | issue = 2 | pages = 326–39 | date = May 2012 | pmid = 22781746 | doi = 10.1016/j.jbior.2012.03.004 }}</ref> α9β1 binding is independent of the RGD peptide sequence. | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{cite journal | author = Evans JP | title = Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. | journal = BioEssays | volume = 23 | issue = 7 | pages = 628–39 | year = 2001 | pmid = 11462216 | doi = 10.1002/bies.1088 }} | |||
*{{cite journal |vauthors=Yamakawa K, Takahashi T, Horio Y, Murata Y, Takahashi E, Hibi K, Yokoyama S, Ueda R, Takahashi T, Nakamura Y | title = Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22. | journal = Oncogene | volume = 8 | issue = 2 | pages = 327–30 | year = 1993 | pmid = 8381220 | doi = }} | |||
*{{cite journal | *{{cite journal |vauthors=Yokosaki Y, Monis H, Chen J, Sheppard D | title = Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains. | journal = J. Biol. Chem. | volume = 271 | issue = 39 | pages = 24144–50 | year = 1996 | pmid = 8798654 | doi = 10.1074/jbc.271.39.24144 }} | ||
*{{cite journal | *{{cite journal |vauthors=Yokosaki Y, Matsuura N, Sasaki T, Murakami I, Schneider H, Higashiyama S, Saitoh Y, Yamakido M, Taooka Y, Sheppard D | title = The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. | journal = J. Biol. Chem. | volume = 274 | issue = 51 | pages = 36328–34 | year = 2000 | pmid = 10593924 | doi = 10.1074/jbc.274.51.36328 }} | ||
*{{cite journal |vauthors=Young BA, Taooka Y, Liu S, Askins KJ, Yokosaki Y, Thomas SM, Sheppard D | title = The cytoplasmic domain of the integrin alpha9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner. | journal = Mol. Biol. Cell | volume = 12 | issue = 10 | pages = 3214–25 | year = 2002 | pmid = 11598204 | pmc = 60168 | doi = 10.1091/mbc.12.10.3214 }} | |||
*{{cite journal |vauthors=Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y | title = Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. | journal = J. Biol. Chem. | volume = 277 | issue = 20 | pages = 17804–10 | year = 2002 | pmid = 11882657 | doi = 10.1074/jbc.M200086200 }} | |||
*{{cite journal | *{{cite journal |vauthors=Majumdar M, Tarui T, Shi B, Akakura N, Ruf W, Takada Y | title = Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1). | journal = J. Biol. Chem. | volume = 279 | issue = 36 | pages = 37528–34 | year = 2004 | pmid = 15247268 | doi = 10.1074/jbc.M401372200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Chen C, Young BA, Coleman CS, Pegg AE, Sheppard D | title = Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration. | journal = J. Cell Biol. | volume = 167 | issue = 1 | pages = 161–70 | year = 2004 | pmid = 15479742 | pmc = 2172529 | doi = 10.1083/jcb.200312166 }} | ||
*{{cite journal | *{{cite journal |vauthors=Vlahakis NE, Young BA, Atakilit A, Sheppard D | title = The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1. | journal = J. Biol. Chem. | volume = 280 | issue = 6 | pages = 4544–52 | year = 2005 | pmid = 15590642 | pmc = 1368959 | doi = 10.1074/jbc.M412816200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Yokosaki Y, Tanaka K, Higashikawa F, Yamashita K, Eboshida A | title = Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin. | journal = Matrix Biol. | volume = 24 | issue = 6 | pages = 418–27 | year = 2005 | pmid = 16005200 | doi = 10.1016/j.matbio.2005.05.005 }} | ||
*{{cite journal | *{{cite journal |vauthors=Gulubova M, Vlaykova T | title = Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases. | journal = Acta Histochem. | volume = 108 | issue = 1 | pages = 25–35 | year = 2006 | pmid = 16430945 | doi = 10.1016/j.acthis.2005.12.001 }} | ||
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{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | *[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3680 ITGA9] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway] | ||
{{Integrins}} | |||
[[Category:Integrins]] | |||
{{gene-3-stub}} |
Latest revision as of 16:50, 16 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene.[1][2][3]
Function
This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for tenascin-C, VCAM1 and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.[3]
Interactions
The α9 subunit forms a heterodimeric complex with a β1 subunit to form the α9β1 integrin. This integrin participates in cell adhesion with various ligands in the extracellular matrix (ECM), including extra domain A (EDA) fibronectin, tenascin-C, ADAMs, EMELIN1, osteopontin, and VEGF.[4] α9β1 binding is independent of the RGD peptide sequence.
References
- ↑ Palmer EL, Rüegg C, Ferrando R, Pytela R, Sheppard D (Jan 1994). "Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle". J Cell Biol. 123 (5): 1289–97. doi:10.1083/jcb.123.5.1289. PMC 2119880. PMID 8245132.
- ↑ Hibi K, Yamakawa K, Ueda R, Horio Y, Murata Y, Tamari M, Uchida K, Takahashi T, Nakamura Y, Takahashi T (Feb 1994). "Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer". Oncogene. 9 (2): 611–9. PMID 8290272.
- ↑ 3.0 3.1 "Entrez Gene: ITGA9 integrin, alpha 9".
- ↑ Høye AM, Couchman JR, Wewer UM, Fukami K, Yoneda A (May 2012). "The newcomer in the integrin family: integrin α9 in biology and cancer". Advances in biological regulation. 52 (2): 326–39. doi:10.1016/j.jbior.2012.03.004. PMID 22781746.
Further reading
- Evans JP (2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization". BioEssays. 23 (7): 628–39. doi:10.1002/bies.1088. PMID 11462216.
- Yamakawa K, Takahashi T, Horio Y, Murata Y, Takahashi E, Hibi K, Yokoyama S, Ueda R, Takahashi T, Nakamura Y (1993). "Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22". Oncogene. 8 (2): 327–30. PMID 8381220.
- Yokosaki Y, Monis H, Chen J, Sheppard D (1996). "Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains". J. Biol. Chem. 271 (39): 24144–50. doi:10.1074/jbc.271.39.24144. PMID 8798654.
- Yokosaki Y, Matsuura N, Sasaki T, Murakami I, Schneider H, Higashiyama S, Saitoh Y, Yamakido M, Taooka Y, Sheppard D (2000). "The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin". J. Biol. Chem. 274 (51): 36328–34. doi:10.1074/jbc.274.51.36328. PMID 10593924.
- Young BA, Taooka Y, Liu S, Askins KJ, Yokosaki Y, Thomas SM, Sheppard D (2002). "The cytoplasmic domain of the integrin alpha9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner". Mol. Biol. Cell. 12 (10): 3214–25. doi:10.1091/mbc.12.10.3214. PMC 60168. PMID 11598204.
- Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions". J. Biol. Chem. 277 (20): 17804–10. doi:10.1074/jbc.M200086200. PMID 11882657.
- Majumdar M, Tarui T, Shi B, Akakura N, Ruf W, Takada Y (2004). "Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1)". J. Biol. Chem. 279 (36): 37528–34. doi:10.1074/jbc.M401372200. PMID 15247268.
- Chen C, Young BA, Coleman CS, Pegg AE, Sheppard D (2004). "Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration". J. Cell Biol. 167 (1): 161–70. doi:10.1083/jcb.200312166. PMC 2172529. PMID 15479742.
- Vlahakis NE, Young BA, Atakilit A, Sheppard D (2005). "The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1". J. Biol. Chem. 280 (6): 4544–52. doi:10.1074/jbc.M412816200. PMC 1368959. PMID 15590642.
- Yokosaki Y, Tanaka K, Higashikawa F, Yamashita K, Eboshida A (2005). "Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin". Matrix Biol. 24 (6): 418–27. doi:10.1016/j.matbio.2005.05.005. PMID 16005200.
- Gulubova M, Vlaykova T (2006). "Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases". Acta Histochem. 108 (1): 25–35. doi:10.1016/j.acthis.2005.12.001. PMID 16430945.
External links
- ITGA9 Info with links in the Cell Migration Gateway
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