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TGF beta receptor

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transforming growth factor beta, receptor type I (activin A receptor type II-like kinase, 53kDa)
Identifiers
SymbolTGFBR1
Alt. symbolsALK5
NCBI gene7046
HGNC11772
OMIM190181
RefSeqNM_004612
UniProtP36897
Other data
LocusChr. 9 q22
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StructuresSwiss-model
DomainsInterPro
transforming growth factor beta, receptor type II (70/80kDa)
Identifiers
SymbolTGFBR2
Alt. symbolsMFS2
NCBI gene7048
HGNC11773
OMIM190182
RefSeqNM_001024847
UniProtP37173
Other data
LocusChr. 3 p24.1
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StructuresSwiss-model
DomainsInterPro
transforming growth factor beta, receptor type III
Identifiers
SymbolTGFBR3
Alt. symbolsβ-Glycan
NCBI gene7049
HGNC11774
OMIM600742
RefSeqNM_003243
UniProtQ03167
Other data
LocusChr. 1 p33-p32
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StructuresSwiss-model
DomainsInterPro

Transforming growth factor beta (TGFβ) receptors are single pass serine/threonine kinase receptors that belong to TGFβ receptor family. 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, bone, 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.[citation needed]

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

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References

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  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. doi:10.1016/S0021-9258(18)37487-8. PMID 2903157.
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