TGF beta receptors

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transforming growth factor beta, receptor type I (activin A receptor type II-like kinase, 53kDa)
Identifiers
Symbol TGFBR1
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
Entrez 7049
HUGO 11774
OMIM 600742
RefSeq NM_003243
UniProt Q03167
Other data
Locus Chr. 1 p33-p32

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.

TGF (Transforming Growth Factor) are involved in paracrine signalling and can be found in many different tissue types, including brain, heart, kidney, liver, and testes. Over-expression of TGF can induce renal fibrosis, causing kidney disease, as well as diabetes, and ultimately end-stage renal disease (ESRD). 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.

Classification[edit]

Three TGF-β receptor types can be distinguished by their structural and functional properties. Receptor types I and II have similar ligand-binding affinities and can be distinguished from each other only by peptide mapping. Both receptor types I and II have a high affinity for TGF-β1 and low affinity for TGF-β2. TGF-β receptor type III has a high affinity for both TGF-β1 and -β2 and in addition TGF-β1.2.[2]

Types[edit]

References[edit]

  1. ^ Doré Jr, J. J.; Edens, M.; Garamszegi, N.; Leof, E. B. (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): 31770–31777. doi:10.1074/jbc.273.48.31770. PMID 9822641.  (free full text)
  2. ^ Cheifetz, S.; Andres, J. L.; Massagué, J. (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): 16984–16991. PMID 2903157. 

External links[edit]