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• W2891991957 abstract "Cell surface receptors must specifically recognize an extracellular ligand and then trigger an appropriate response within the cell. Their general structure enables this, as it comprises an extracellular domain that can bind an extracellular ligand, a cytoplasmic domain that can transduce a signal inside the cell to produce an appropriate response, and a transmembrane domain that links the two and is responsible for accurately delivering specific information on a binding event from the extracellular domain to the cytoplasmic domain, to trigger the proper response. A vast body of research has focused on elucidating the specific mechanisms responsible for regulating extracellular binding events and the subsequent interactions of the cytoplasmic domain with intracellular signaling. In contrast, far less work has focused on examining how the transmembrane domain links these domains and delivers the necessary information. In this review, we propose the importance of the transmembrane domain as a signal regulator. We highlight the cell adhesion receptor, syndecan, as a special case, and propose that the transmembrane domain-mediated oligomerization of the syndecan cytoplasmic domain is a unique regulatory mechanism in syndecan signaling." @default.
• W2891991957 created "2018-09-27" @default.
• W2891991957 creator A5033802264 @default.
• W2891991957 creator A5035485431 @default.
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• W2891991957 date "2018-12-01" @default.
• W2891991957 modified "2023-10-01" @default.
• W2891991957 title "Syndecan transmembrane domain modulates intracellular signaling by regulating the oligomeric status of the cytoplasmic domain" @default.
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• W2891991957 doi "https://doi.org/10.1016/j.cellsig.2018.09.003" @default.
• W2891991957 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30195038" @default.
• W2891991957 hasPublicationYear "2018" @default.
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