Biology:ACVR2A
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Activin receptor type-2A is a protein that in humans is encoded by the ACVR2A gene.[1][2][3]
ACVR2A is an activin type 2 receptor.
Function
This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.[3]
Interactions
ACVR2A has been shown to interact with:
References
- ↑ "Molecular cloning and binding properties of the human type II activin receptor". Biochem. Biophys. Res. Commun. 184 (1): 310–6. May 1992. doi:10.1016/0006-291X(92)91194-U. PMID 1314589.
- ↑ "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH". Cytogenet. Cell Genet. 87 (3–4): 219–20. April 2000. doi:10.1159/000015429. PMID 10702675.
- ↑ 3.0 3.1 "Entrez Gene: ACVR2A activin A receptor, type IIA". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92.
- ↑ "Roles of pathway-specific and inhibitory Smads in activin receptor signaling". Mol. Endocrinol. 13 (1): 15–23. January 1999. doi:10.1210/mend.13.1.0218. PMID 9892009.
- ↑ "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. May 1996. doi:10.1006/excr.1996.0142. PMID 8612709.
- ↑ "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature 404 (6776): 411–4. March 2000. doi:10.1038/35006129. PMID 10746731. Bibcode: 2000Natur.404..411L.
- ↑ "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". Endocrinology 138 (7): 2928–36. July 1997. doi:10.1210/endo.138.7.5250. PMID 9202237.
- ↑ "Novel factors in regulation of activin signaling". Mol. Cell. Endocrinol. 225 (1–2): 1–8. October 2004. doi:10.1016/j.mce.2004.02.006. PMID 15451561.
- ↑ "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. 277 (21): 19008–18. May 2002. doi:10.1074/jbc.M112472200. PMID 11882656.
External links
- Human ACVR2A genome location and ACVR2A gene details page in the UCSC Genome Browser.
Further reading
- "The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction". Curr. Opin. Obstet. Gynecol. 14 (3): 317–23. 2002. doi:10.1097/00001703-200206000-00012. PMID 12032389.
- "Cloning of the human activin receptor cDNA reveals high evolutionary conservation". Biochim. Biophys. Acta 1130 (1): 105–8. 1992. doi:10.1016/0167-4781(92)90472-C. PMID 1311955.
- "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell 65 (6): 973–82. 1991. doi:10.1016/0092-8674(91)90549-E. PMID 1646080.
- "Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism". J. Biol. Chem. 270 (11): 6308–13. 1995. doi:10.1074/jbc.270.11.6308. PMID 7890768.
- "Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors". Cell 75 (4): 671–80. 1993. doi:10.1016/0092-8674(93)90488-C. PMID 8242742.
- "Expression of the type II activin receptor gene in the human placenta". Endocrinology 133 (6): 3046–9. 1993. doi:10.1210/endo.133.6.8243335. PMID 8243335.
- "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. 1996. doi:10.1006/excr.1996.0142. PMID 8612709.
- "Activation of signalling by the activin receptor complex". Mol. Cell. Biol. 16 (3): 1066–73. 1996. doi:10.1128/mcb.16.3.1066. PMID 8622651.
- "Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells". Cancer Res. 56 (5): 1155–63. 1996. PMID 8640777.
- "Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5". J. Biol. Chem. 271 (35): 21345–52. 1996. doi:10.1074/jbc.271.35.21345. PMID 8702914.
- "Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation". Mol. Cell. Biol. 17 (3): 1682–91. 1997. doi:10.1128/mcb.17.3.1682. PMID 9032295.
- "Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2". J. Biol. Chem. 273 (40): 25628–36. 1998. doi:10.1074/jbc.273.40.25628. PMID 9748228.
- "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. 274 (2): 584–94. 1999. doi:10.1074/jbc.274.2.584. PMID 9872992.
- "Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1". J. Biol. Chem. 274 (15): 9984–92. 1999. doi:10.1074/jbc.274.15.9984. PMID 10187774.
- "Mutational analysis of activin/transforming growth factor-beta type I and type II receptor kinases in human pituitary tumors". J. Clin. Endocrinol. Metab. 84 (5): 1716–21. 1999. doi:10.1210/jcem.84.5.5704. PMID 10323406.
- "Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation". J. Cell Sci. 112 (20): 3519–27. 1999. doi:10.1242/jcs.112.20.3519. PMID 10504300.
- "Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues". Br. J. Cancer 82 (1): 112–7. 2000. doi:10.1054/bjoc.1999.0886. PMID 10638976.
- "Identification and characterization of a PDZ protein that interacts with activin type II receptors". J. Biol. Chem. 275 (8): 5485–92. 2000. doi:10.1074/jbc.275.8.5485. PMID 10681527.
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