ACVR2B

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Activin A receptor, type IIB
Protein ACVR2B PDB 1nys.png
PDB rendering based on 1nys.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ACVR2B ; ACTRIIB; ActR-IIB; HTX4
External IDs OMIM602730 MGI87912 HomoloGene863 ChEMBL: 5466 GeneCards: ACVR2B Gene
EC number 2.7.11.30
RNA expression pattern
PBB GE ACVR2B 220028 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 93 11481
Ensembl ENSG00000114739 ENSMUSG00000061393
UniProt Q13705 P27040
RefSeq (mRNA) NM_001106 NM_007397
RefSeq (protein) NP_001097 NP_031423
Location (UCSC) Chr 3:
38.5 – 38.53 Mb
Chr 9:
119.4 – 119.43 Mb
PubMed search [1] [2]

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.

Function[edit]

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[edit]

ACVR2B has been shown to interact with ACVR1B[4][5] and SYNJ2BP.[6]

References[edit]

  1. ^ Hildén K, Tuuri T, Erämaa 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. 
  2. ^ Ishikawa S, Kai M, Murata Y, Tamari M, Daigo Y, Murano T et al. (July 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. 
  3. ^ a b "Entrez Gene: ACVR2B activin A receptor, type IIB". 
  4. ^ Attisano L, Wrana J, Montalvo E, Massagué J (March 1996). "Activation of signalling by the activin receptor complex". Mol. Cell. Biol. 16 (3): 1066–73. PMC 231089. PMID 8622651. 
  5. ^ De Winter J, De Vries C, Van Achterberg T, Ameerun R, Feijen A, Sugino H et al. (May 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. 
  6. ^ Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A et al. (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. 277 (21): 19008–18. doi:10.1074/jbc.M112472200. PMID 11882656. 

Further reading[edit]

  • Burdine R, Schier A (2000). "Conserved and divergent mechanisms in left-right axis formation". Genes Dev. 14 (7): 763–76. PMID 10766733. 
  • De Winter J, De Vries C, Van Achterberg T, Ameerun R, Feijen A, Sugino H 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 J, Montalvo E, Massagué J (1996). "Activation of signalling by the activin receptor complex". Mol. Cell. Biol. 16 (3): 1066–73. PMC 231089. PMID 8622651. 
  • Nishitoh H, Ichijo H, Kimura M, Matsumoto T, Makishima F, Yamaguchi A 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 J, de Winter J, Timmerman M, McLuskey A, van Schaik R, Themmen A 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/endo.138.7.5250. PMID 9202237. 
  • Macías-Silva M, Hoodless P, Tang S, Buchwald M, Wrana J (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, Lewin M, Bowers P, Towbin J 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, Ingram D, Milner A (1999). "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. 
  • McPherron A, Lawler A, Lee S (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, Ritvos O, Aaltonen J (1999). "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 S, Woodruff T (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 J, Frank D, Felici A, Green H, Cao Z, Schneider M 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 W, Frank D, Huff C, Renfrew Haft C, Martin J, Meng X 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 K, Kang S, Nathwani P, Cheng K, Auersperg N, Leung P (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 S, McPherron A (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. 
  • Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A 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 M, Manuelpillai U, Waldron K, Dole A, Wallace E (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.