TGF beta receptor
| 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 |
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.
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
- TGFβ superfamily receptor
- TGFβ signaling pathway
- TGFβ superfamily
References
^ 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..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em} (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. PMID 2903157.
External links
TGF-beta+Receptors at the US National Library of Medicine Medical Subject Headings (MeSH)
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