TGF beta receptor 2

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

TGFBR2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTGFBR2, AAT3, FAA3, LDS1B, LDS2, LDS2B, MFS2, RIIC, TAAD2, TGFR-2, TGFbeta-RII, transforming growth factor beta receptor 2, TBR-ii, TBRII
External IDsOMIM: 190182 MGI: 98729 HomoloGene: 2435 GeneCards: TGFBR2
Orthologs
SpeciesHumanMouse
Entrez

7048

21813

Ensembl

ENSG00000163513

ENSMUSG00000032440

UniProt

P37173

Q62312

RefSeq (mRNA)

NM_001024847
NM_003242

NM_009371
NM_029575

RefSeq (protein)

NP_001020018
NP_003233

NP_033397
NP_083851

Location (UCSC)Chr 3: 30.61 – 30.69 MbChr 9: 115.91 – 116 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

It is a tumor suppressor gene.[5]

Function

This gene encodes a member of the serine/threonine 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. At least 73 disease-causing mutations in this gene have been discovered.[6] Alternatively spliced transcript variants encoding different isoforms have been characterized.[7]

Interactions

TGF beta receptor 2 has been shown to interact with:

Domain architecture

Transforming growth factor beta receptor 2 ectodomain
crystal structure of human tgf-beta type ii receptor ligand binding domain
Identifiers
SymbolecTbetaR2
PfamPF08917
InterProIPR015013
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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).[18]

See also

References

  1. GRCh38: Ensembl release 89: ENSG00000163513 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000032440 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Archived from the original on 2011-08-10. Retrieved 2008-09-07.
  6. Šimčíková D, Heneberg P (December 2019). "Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases". Scientific Reports. 9 (1): 18577. Bibcode:2019NatSR...918577S. doi:10.1038/s41598-019-54976-4. PMC 6901466. PMID 31819097.
  7. "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)".
  8. Yao D, Ehrlich M, Henis YI, Leof EB (Nov 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Molecular Biology of the Cell. 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. PMC 133610. PMID 12429842.
  9. Liu JH, Wei S, Burnette PK, Gamero AM, Hutton M, Djeu JY (Jan 1999). "Functional association of TGF-beta receptor II with cyclin B". Oncogene. 18 (1): 269–75. doi:10.1038/sj.onc.1202263. PMID 9926943.
  10. Barbara NP, Wrana JL, Letarte M (Jan 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". The Journal of Biological Chemistry. 274 (2): 584–94. doi:10.1074/jbc.274.2.584. PMID 9872992.
  11. Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, Bernabeu C (Aug 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". The Journal of Biological Chemistry. 277 (32): 29197–209. doi:10.1074/jbc.M111991200. PMID 12015308.
  12. Wrighton KH, Lin X, Feng XH (Jul 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proceedings of the National Academy of Sciences of the United States of America. 105 (27): 9244–9. Bibcode:2008PNAS..105.9244W. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.
  13. Datta PK, Chytil A, Gorska AE, Moses HL (Dec 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". The Journal of Biological Chemistry. 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. PMID 9856985.
  14. Datta PK, Moses HL (May 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Molecular and Cellular Biology. 20 (9): 3157–67. doi:10.1128/mcb.20.9.3157-3167.2000. PMC 85610. PMID 10757800.
  15. Kawabata M, Chytil A, Moses HL (Mar 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". The Journal of Biological Chemistry. 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. PMID 7890683.
  16. Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP (Mar 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". The Journal of Biological Chemistry. 276 (9): 6727–38. doi:10.1074/jbc.M008340200. PMID 11102446.
  17. De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD (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". Journal of Molecular Biology. 328 (5): 1173–83. doi:10.1016/s0022-2836(03)00360-7. PMID 12729750.
  18. Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP (Mar 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nature Structural Biology. 9 (3): 203–8. doi:10.1038/nsb766. PMID 11850637. S2CID 13322593.
  19. Rotzer D, Roth M, Lutz M, Lindemann D, Sebald W, Knaus P (Feb 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". The EMBO Journal. 20 (3): 480–90. doi:10.1093/emboj/20.3.480. PMC 133482. PMID 11157754.
This article incorporates text from the public domain Pfam and InterPro: IPR015013
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