AMOT
From Wikidoc - Reading time: 4 min
| Angiomotin | |||||||||||
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| Identifiers | |||||||||||
| Symbols | AMOT ; KIAA1071 | ||||||||||
| External IDs | Template:OMIM5 | ||||||||||
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| Species | Human | Mouse | |||||||||
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| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
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Angiomotin, also known as AMOT, is a human gene.[1]
This gene belongs to the motin family of angiostatin binding proteins characterized by conserved coiled-coil domains and C-terminal PDZ binding motifs. The encoded protein is expressed predominantly in endothelial cells of capillaries as well as larger vessels of the placenta where it may mediate the inhibitory effect of angiostatin on tube formation and the migration of endothelial cells toward growth factors during the formation of new blood vessels. Alternatively spliced transcript variants encoding different isoforms have been described, but their full-length nature has not been completely determined.[1]
References[edit | edit source]
Further reading[edit | edit source]
- Nakajima D, Okazaki N, Yamakawa H; et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. PMID 12168954.
- Kikuno R, Nagase T, Ishikawa K; et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. PMID 10470851.
- Troyanovsky B, Levchenko T, Månsson G; et al. (2001). "Angiomotin: an angiostatin binding protein that regulates endothelial cell migration and tube formation". J. Cell Biol. 152 (6): 1247–54. PMID 11257124.
- Zetter BR (2001). "Hold that line. Angiomotin regulates endothelial cell motility". J. Cell Biol. 152 (6): F35–6. PMID 11257132.
- Bratt A, Wilson WJ, Troyanovsky B; et al. (2003). "Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains". Gene. 298 (1): 69–77. PMID 12406577.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Levchenko T, Aase K, Troyanovsky B; et al. (2004). "Loss of responsiveness to chemotactic factors by deletion of the C-terminal protein interaction site of angiomotin". J. Cell. Sci. 116 (Pt 18): 3803–10. doi:10.1242/jcs.00694. PMID 12902404.
- Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Moreau J, Lord M, Boucher M; et al. (2005). "Protein diversity is generated within the motin family of proteins by alternative pre-mRNA splicing". Gene. 350 (2): 137–48. doi:10.1016/j.gene.2005.02.001. PMID 15804419.
- Bratt A, Birot O, Sinha I; et al. (2005). "Angiomotin regulates endothelial cell-cell junctions and cell motility". J. Biol. Chem. 280 (41): 34859–69. doi:10.1074/jbc.M503915200. PMID 16043488.
- Ernkvist M, Aase K, Ukomadu C; et al. (2006). "p130-angiomotin associates to actin and controls endothelial cell shape". FEBS J. 273 (9): 2000–11. doi:10.1111/j.1742-4658.2006.05216.x. PMID 16640563.
- Wells CD, Fawcett JP, Traweger A; et al. (2006). "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells". Cell. 125 (3): 535–48. doi:10.1016/j.cell.2006.02.045. PMID 16678097.
- Holmgren L, Ambrosino E, Birot O; et al. (2006). "A DNA vaccine targeting angiomotin inhibits angiogenesis and suppresses tumor growth". Proc. Natl. Acad. Sci. U.S.A. 103 (24): 9208–13. doi:10.1073/pnas.0603110103. PMID 16754857.
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