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.
| transforming growth factor beta, receptor type I (activin A receptor type II-like kinase, 53kDa) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | TGFBR1 | ||||||
| Alt. symbols | ALK5 | ||||||
| NCBI gene | 7046 | ||||||
| HGNC | 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 | ||||||
| NCBI gene | 7048 | ||||||
| HGNC | 11773 | ||||||
| OMIM | 190182 | ||||||
| RefSeq | NM_001024847 | ||||||
| UniProt | P37173 | ||||||
| Other data | |||||||
| Locus | Chr. 3 p24.1 | ||||||
| |||||||
| transforming growth factor beta, receptor type III | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | TGFBR3 | ||||||
| Alt. symbols | β-Glycan | ||||||
| NCBI gene | 7049 | ||||||
| HGNC | 11774 | ||||||
| OMIM | 600742 | ||||||
| RefSeq | NM_003243 | ||||||
| UniProt | Q03167 | ||||||
| Other data | |||||||
| Locus | Chr. 1 p33-p32 | ||||||
| |||||||
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
editReferences
edit- ^ 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)
- ^ 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.
External links
edit- TGF-beta+Receptors at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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