TGF-beta receptor: Difference between revisions
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== Function == | == Function == | ||
'''TGF-β receptors''' (Transforming Growth Factor) (TGFR) are serine/threonine kinase receptors. They are involved in paracrine signaling and are found in many types of tissue. TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β<ref>PMID:9525694</ref>. There are 3 types of TGFR: <br /> | '''TGF-β receptors''' (Transforming Growth Factor) (TGFR) are [[serine/threonine kinase]] receptors. They are involved in paracrine signaling and are found in many types of tissue. TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β<ref>PMID:9525694</ref>. There are 3 types of TGFR: <br /> | ||
*'''TGFR I''' forms heteromeric complex with TGFR II when it is bound to TGF-β. The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation. TGFR I has high affinity for TGF-β1 and low affinity for TGF-β2. <br /> | *'''TGFR I''' forms heteromeric complex with TGFR II when it is bound to TGF-β. The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation. TGFR I has high affinity for TGF-β1 and low affinity for TGF-β2. <br /> | ||
*'''TGFR II''' is a tumor suppressor transmembrane protein. TGFR II has high affinity for TGF-β1 and low affinity for TGF-β2. <br /> | *'''TGFR II''' is a tumor suppressor transmembrane protein. TGFR II has high affinity for TGF-β1 and low affinity for TGF-β2. <br /> | ||
*'''TGFR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan. It acts as a reservoir of ligand for TGFRs. TGFR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2. | *'''TGFR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan. It acts as a reservoir of ligand for TGFRs. TGFR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2. | ||
See also [[Receptor]] and [[Growth factors]]. | See also [[Receptor]], [[TGF beta signaling pathway]], and [[Growth factors]]. | ||
== Disease == | == Disease == | ||
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TGFR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain; a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization. | TGFR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain; a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization. | ||
== 3D Structures of TGF- | == 3D Structures of TGF-beta receptor== | ||
[[TGF- | [[TGF-beta receptor 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 06:19, 2 October 2022
FunctionTGF-β receptors (Transforming Growth Factor) (TGFR) are serine/threonine kinase receptors. They are involved in paracrine signaling and are found in many types of tissue. TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β[1]. There are 3 types of TGFR:
See also Receptor, TGF beta signaling pathway, and Growth factors. DiseaseOver-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFR II cause various types of tumors[2]. Structural highlightsTGFR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain; a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization. 3D Structures of TGF-beta receptorTGF-beta receptor 3D structures
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ReferencesReferences
- ↑ Wrana JL. TGF-beta receptors and signalling mechanisms. Miner Electrolyte Metab. 1998;24(2-3):120-30. PMID:9525694
- ↑ Frischmeyer-Guerrerio PA, Guerrerio AL, Oswald G, Chichester K, Myers L, Halushka MK, Oliva-Hemker M, Wood RA, Dietz HC. TGFbeta receptor mutations impose a strong predisposition for human allergic disease. Sci Transl Med. 2013 Jul 24;5(195):195ra94. doi: 10.1126/scitranslmed.3006448. PMID:23884466 doi:http://dx.doi.org/10.1126/scitranslmed.3006448