TGF beta receptor

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transforming growth factor beta, receptor type I (activin A receptor type II-like kinase, 53kDa)
Identifiers
Symbol TGFBR1
Alt. symbols ALK5
Entrez 7046
HUGO 11772
OMIM 190181
RefSeq NM_004612
UniProt P36897
Other data
Locus Chr. 9 q22
transforming growth factor beta, receptor type II (70/80kDa)
Identifiers
Symbol TGFBR2
Alt. symbols MFS2
Entrez 7048
HUGO 11773
OMIM 190182
RefSeq NM_001024847
UniProt P37173
Other data
Locus Chr. 3 p22
transforming growth factor beta, receptor type III
Identifiers
Symbol TGFBR3
Alt. symbols β-Glycan
Entrez 7049
HUGO 11774
OMIM 600742
RefSeq NM_003243
UniProt Q03167
Other data
Locus Chr. 1 p33-p32
Not to be confused with TGFβ superfamily receptor.

Transforming growth factor beta (TGFβ) receptors are single pass serine/threonine kinase receptors. They exist in several different isoforms that can be homo- or heterodimeric.[1] The number of characterized ligands in the TGFβ superfamily far exceeds the number of known receptors, suggesting the promiscuity that exists between the ligand and receptor interactions.

TGFβ is a growth factor and cytokine involved in paracrine signalling and can be found in many different tissue types, including brain, heart, kidney, liver, and testes. Over-expression of TGFβ can induce renal fibrosis, causing kidney disease, as well as diabetes, and ultimately end-stage renal disease. Recent developments have found that, using certain types of protein antagonists against TGFβ receptors, can halt and in some cases reverse the effects of renal fibrosis.

Three TGFβ superfamily receptors specific for TGFβ, the TGFβ receptors, can be distinguished by their structural and functional properties. TGFβR1 (ALK5) and TGFβR2 have similar ligand-binding affinities and can be distinguished from each other only by peptide mapping. Both TGFβR1 and TGFβR2 have a high affinity for TGFβ1 and low affinity for TGFβ2. TGFβR3 (β-glycan) has a high affinity for both homodimeric TGFβ1 and TGFβ2 and in addition the heterodimer TGF-β1.2.[2] The TGFβ receptors also bind TGFβ3.

See also[edit]

References[edit]

  1. ^ Doré JJ, Edens M, Garamszegi N, Leof EB (November 1998). "Heteromeric and homomeric transforming growth factor-beta receptors show distinct signaling and endocytic responses in epithelial cells". The Journal of Biological Chemistry 273 (48): 31770–7. doi:10.1074/jbc.273.48.31770. PMID 9822641.  (free full text)
  2. ^ Cheifetz S, Andres JL, Massagué J (November 1988). "The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor". The Journal of Biological Chemistry 263 (32): 16984–91. PMID 2903157. 

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