Angiomotin

Angiomotin
Identifiers
Symbols	AMOT ; KIAA1071
External IDs	OMIM: 300410 HomoloGene: 15778 GeneCards: AMOT Gene
Gene ontology Molecular function • receptor activity • protein binding • angiostatin binding Cellular component • stress fiber • ruffle • cytoplasm • cytosol • actin filament • bicellular tight junction • COP9 signalosome • external side of plasma membrane • cell surface • integral component of membrane • lamellipodium • endocytic vesicle Biological process • vasculogenesis • in utero embryonic development • gastrulation with mouth forming second • establishment of cell polarity involved in ameboidal cell migration • chemotaxis • cell-cell junction assembly • negative regulation of angiogenesis • actin cytoskeleton organization • regulation of cell migration • negative regulation of GTPase activity • cellular protein localization • hippo signaling • positive regulation of embryonic development • cell migration involved in gastrulation • negative regulation of vascular permeability • blood vessel endothelial cell migration • positive regulation of blood vessel endothelial cell migration • positive regulation of cell size • regulation of small GTPase mediated signal transduction • positive regulation of stress fiber assembly Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	154796	27494
Ensembl	ENSG00000126016	ENSMUSG00000041688
UniProt	Q4VCS5	Q8VHG2
RefSeq (mRNA)	NM_001113490	NM_001290274
RefSeq (protein)	NP_001106962	NP_001277203
Location (UCSC)	Chr X: 112.77 – 112.84 Mb	Chr X: 145.45 – 145.51 Mb
PubMed search

Angiomotin is a protein that in humans is encoded by the AMOT gene.^[1][2][3][4]

Function

Angiomotin is a 675-residue protein that increases the random migration of endothelial cells as well as the migration of endothelial cells toward growth factors.

In the presence of angiostatin, endothelial cells that overexpress angiomotin exhibit a significant reduction in migration toward growth factors as well as an inability to form tubules in vitro. These observations are consistent with the localization of angiomotin in the leading edge of migrating cells. Angiostatin, therefore, disrupts the normal migratory function of Angiomotin.

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.^[4]

References

1. Troyanovsky B, Levchenko T, Mansson G, Matvijenko O, Holmgren L (Mar 2001). "Angiomotin: An Angiostatin Binding Protein That Regulates Endothelial Cell Migration and Tube Formation". J Cell Biol 152 (6): 1247–54. doi:10.1083/jcb.152.6.1247. PMC 2199208. PMID 11257124.
2. Bratt A, Birot O, Sinha I, Veitonmaki N, Aase K, Ernkvist M, Holmgren L (Oct 2005). "Angiomotin regulates endothelial cell-cell junctions and cell motility". J Biol Chem 280 (41): 34859–69. doi:10.1074/jbc.M503915200. PMID 16043488.
3. Bratt A, Wilson WJ, Troyanovsky B, Aase K, Kessler R, Van Meir EG, Holmgren L (Oct 2002). "Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains". Gene 298 (1): 69–77. doi:10.1016/S0378-1119(02)00928-9. PMID 12406577.
4. "Entrez Gene: AMOT angiomotin".

Further reading

• Zetter BR (2001). "Hold That Line: Angiomotin Regulates Endothelial Cell Motility". J. Cell Biol. 152 (6): F35–6. doi:10.1083/jcb.152.6.F35. PMC 2199203. PMID 11257132.
• 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.
• 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.
• 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. PMC 1482591. PMID 16754857.