Open Access Articles- Top Results for TGF beta receptor 2

TGF beta receptor 2

External IDsOMIM190182 MGI98729 HomoloGene2435 IUPHAR: 1795 ChEMBL: 4267 GeneCards: TGFBR2 Gene
EC number2.7.11.30
RNA expression pattern
File:PBB GE TGFBR2 208944 at tn.png
File:PBB GE TGFBR2 207334 s at tn.png
More reference expression data
RefSeq (mRNA)NM_001024847NM_009371
RefSeq (protein)NP_001020018NP_033397
Location (UCSC)Chr 3:
30.65 – 30.74 Mb
Chr 9:
116.09 – 116.18 Mb
PubMed search[1][2]

Transforming growth factor, beta receptor II (70/80kDa) is a TGF beta receptor. TGFBR2 is its human gene.

It is a tumor suppressor gene.[1]

This gene encodes a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. The encoded protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated with Marfan syndrome, Loeys-Deitz aortic aneurysm syndrome, Osler-Weber-Rendu syndrome, and the development of various types of tumors. Alternatively spliced transcript variants encoding different isoforms have been characterized.[2]


TGF beta receptor 2 has been shown to interact with Cyclin B2,[3] TGF beta receptor 1,[4][5] Transforming growth factor, beta 3,[6][7][8][9] AP2B1,[10] Endoglin,[8][11] Heat shock protein 90kDa alpha (cytosolic), member A1[12] and STRAP.[13][14]

Domain architecture

Transforming growth factor beta receptor 2 ectodomain
File:PDB 1m9z EBI.jpg
crystal structure of human tgf-beta type ii receptor ligand binding domain
Symbol ecTbetaR2
Pfam PF08917
InterPro IPR015013

TGF beta receptor 2 consists of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9).[7]

See also

External links


  1. ^ "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Retrieved 2008-09-07. 
  2. ^ "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)". 
  3. ^ Liu, J H; Wei S; Burnette P K; Gamero A M; Hutton M; Djeu J Y (January 1999). "Functional association of TGF-beta receptor II with cyclin B". Oncogene (ENGLAND) 18 (1): 269–75. ISSN 0950-9232. PMID 9926943. doi:10.1038/sj.onc.1202263. 
  4. ^ Kawabata, M; Chytil A; Moses H L (March 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". J. Biol. Chem. (UNITED STATES) 270 (10): 5625–30. ISSN 0021-9258. PMID 7890683. doi:10.1074/jbc.270.10.5625. 
  5. ^ Razani, B; Zhang X L; Bitzer M; von Gersdorff G; Böttinger E P; Lisanti M P (March 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". J. Biol. Chem. (United States) 276 (9): 6727–38. ISSN 0021-9258. PMID 11102446. doi:10.1074/jbc.M008340200. 
  6. ^ De Crescenzo, Gregory; Pham Phuong L, Durocher Yves, O'Connor-McCourt Maureen D (May 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding". J. Mol. Biol. (England) 328 (5): 1173–83. ISSN 0022-2836. PMID 12729750. doi:10.1016/S0022-2836(03)00360-7. 
  7. ^ a b Hart, P John; Deep Shashank; Taylor Alexander B; Shu Zhanyong; Hinck Cynthia S; Hinck Andrew P (March 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nat. Struct. Biol. (United States) 9 (3): 203–8. ISSN 1072-8368. PMID 11850637. doi:10.1038/nsb766. 
  8. ^ a b Barbara, N P; Wrana J L; Letarte M (January 1999). "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. (UNITED STATES) 274 (2): 584–94. ISSN 0021-9258. PMID 9872992. doi:10.1074/jbc.274.2.584. 
  9. ^ Rotzer, D; Roth M; Lutz M; Lindemann D; Sebald W; Knaus P (February 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". EMBO J. (England) 20 (3): 480–90. ISSN 0261-4189. PMC 133482. PMID 11157754. doi:10.1093/emboj/20.3.480. 
  10. ^ Yao, Diying; Ehrlich Marcelo; Henis Yoav I; Leof Edward B (November 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Mol. Biol. Cell (United States) 13 (11): 4001–12. ISSN 1059-1524. PMC 133610. PMID 12429842. doi:10.1091/mbc.02-07-0104. 
  11. ^ Guerrero-Esteo, Mercedes; Sanchez-Elsner Tilman, Letamendia Ainhoa, Bernabeu Carmelo (August 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". J. Biol. Chem. (United States) 277 (32): 29197–209. ISSN 0021-9258. PMID 12015308. doi:10.1074/jbc.M111991200. 
  12. ^ Wrighton, Katharine H; Lin Xia; Feng Xin-Hua (July 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (27): 9244–9. PMC 2453700. PMID 18591668. doi:10.1073/pnas.0800163105. 
  13. ^ Datta, P K; Chytil A; Gorska A E; Moses H L (Dec 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". J. Biol. Chem. (UNITED STATES) 273 (52): 34671–4. ISSN 0021-9258. PMID 9856985. doi:10.1074/jbc.273.52.34671. 
  14. ^ Datta, P K; Moses H L (May 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Mol. Cell. Biol. (UNITED STATES) 20 (9): 3157–67. ISSN 0270-7306. PMC 85610. PMID 10757800. doi:10.1128/MCB.20.9.3157-3167.2000. 

This article incorporates text from the public domain Pfam and InterPro IPR015013