ACVR2B
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ACVR2B
Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene.[1][2][3] ACVR2B is an activin type 2 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. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor.[3]
Interactions
ACVR2B has been shown to interact with SYNJ2BP[4] and ACVR1B.[5][6]
References
- ^ Hilden K, Tuuri T, Eramaa M, Ritvos O (May 1994). "Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor". Blood 83 (8): 2163–70. PMID 8161782.
- ^ Ishikawa S, Kai M, Murata Y, Tamari M, Daigo Y, Murano T, Ogawa M, Nakamura Y (Jul 1998). "Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene". J Hum Genet 43 (2): 132–4. doi:10.1007/s100380050054. PMID 9621519.
- ^ a b "Entrez Gene: ACVR2B activin A receptor, type IIB". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=93.
- ^ Matsuzaki, Takashi; Hanai Sayuri, Kishi Hisashi, Liu ZhongHui, Bao YongLi, Kikuchi Akira, Tsuchida Kunihiro, Sugino Hiromu (May. 2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. (United States) 277 (21): 19008–18. doi:10.1074/jbc.M112472200. ISSN 0021-9258. PMID 11882656.
- ^ Attisano, L; Wrana J L, Montalvo E, Massagué J (Mar. 1996). "Activation of signalling by the activin receptor complex". Mol. Cell. Biol. (UNITED STATES) 16 (3): 1066–73. ISSN 0270-7306. PMC 231089. PMID 8622651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231089.
- ^ De Winter, J P; De Vries C J, Van Achterberg T A, Ameerun R F, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij A J (May. 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. (UNITED STATES) 224 (2): 323–34. doi:10.1006/excr.1996.0142. ISSN 0014-4827. PMID 8612709.
Further reading
- Burdine RD, Schier AF (2000). "Conserved and divergent mechanisms in left-right axis formation.". Genes Dev. 14 (7): 763–76. PMID 10766733.
- De Winter JP, De Vries CJ, Van Achterberg TA, et al. (1996). "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. doi:10.1006/excr.1996.0142. PMID 8612709.
- Attisano L, Wrana JL, Montalvo E, Massagué J (1996). "Activation of signalling by the activin receptor complex.". Mol. Cell. Biol. 16 (3): 1066–73. PMC 231089. PMID 8622651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231089.
- Nishitoh H, Ichijo H, Kimura M, et al. (1996). "Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5.". J. Biol. Chem. 271 (35): 21345–52. doi:10.1074/jbc.271.35.21345. PMID 8702914.
- Martens JW, de Winter JP, Timmerman MA, et al. (1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells.". Endocrinology 138 (7): 2928–36. doi:10.1210/en.138.7.2928. PMID 9202237.
- Macías-Silva M, Hoodless PA, Tang SJ, et al. (1998). "Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2.". J. Biol. Chem. 273 (40): 25628–36. doi:10.1074/jbc.273.40.25628. PMID 9748228.
- Kosaki R, Gebbia M, Kosaki K, et al. (1999). "Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB.". Am. J. Med. Genet. 82 (1): 70–6. doi:10.1002/(SICI)1096-8628(19990101)82:1<70::AID-AJMG14>3.0.CO;2-Y. PMID 9916847.
- Lee S, Alexander J, Blowes R, et al. (2000). "Determination of resonance frequency of the respiratory system in respiratory distress syndrome.". Arch. Dis. Child. Fetal Neonatal Ed. 80 (3): F198–202. doi:10.1136/fn.80.3.F198. PMC 1720943. PMID 10212081. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1720943.
- McPherron AC, Lawler AM, Lee SJ (1999). "Regulation of anterior/posterior patterning of the axial skeleton by growth/differentiation factor 11.". Nat. Genet. 22 (3): 260–4. doi:10.1038/10320. PMID 10391213.
- Bondestam J, Horelli-Kuitunen N, Hildén K, et al. (2000). "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. doi:10.1159/000015429. PMID 10702675.
- Chapman SC, Woodruff TK (2001). "Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP).". Mol. Endocrinol. 15 (4): 668–79. doi:10.1210/me.15.4.668. PMID 11266516.
- Wurthner JU, Frank DB, Felici A, et al. (2001). "Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone.". J. Biol. Chem. 276 (22): 19495–502. doi:10.1074/jbc.M006473200. PMID 11278302.
- Parks WT, Frank DB, Huff C, et al. (2001). "Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases.". J. Biol. Chem. 276 (22): 19332–9. doi:10.1074/jbc.M100606200. PMID 11279102.
- Choi KC, Kang SK, Nathwani PS, et al. (2001). "Differential expression of activin/inhibin subunit and activin receptor mRNAs in normal and neoplastic ovarian surface epithelium (OSE).". Mol. Cell. Endocrinol. 174 (1-2): 99–110. doi:10.1016/S0303-7207(00)00447-0. PMID 11306176.
- Lee SJ, McPherron AC (2001). "Regulation of myostatin activity and muscle growth.". Proc. Natl. Acad. Sci. U.S.A. 98 (16): 9306–11. doi:10.1073/pnas.151270098. PMC 55416. PMID 11459935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55416.
- Matsuzaki T, Hanai S, Kishi H, et al. (2002). "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. doi:10.1074/jbc.M112472200. PMID 11882656.
- Schneider-Kolsky ME, Manuelpillai U, Waldron K, et al. (2002). "The distribution of activin and activin receptors in gestational tissues across human pregnancy and during labour.". Placenta 23 (4): 294–302. doi:10.1053/plac.2002.0787. PMID 11969340.
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