Syndecan transmembrane domain modulates intracellular signaling by regulating the oligomeric status of the cytoplasmic domain
- 주제(키워드) Syndecan , Receptor , Transmembrane domain , Signal transduction , Dimerization
- 주제(기타) Cell Biology
- 설명문(일반) [Jang, Bohee; Hong, Heejeong; Oh, Eok-Soo] Ewha Womans Univ, Res Ctr Cellular Homeostasis, Dept Life Sci, Seoul 120750, South Korea; [Jung, Hyejung; Oh, Eok-Soo] Skin QC Inst Dermatol Sci, Seoul 03759, South Korea
- 등재 SCIE, SCOPUS
- 발행기관 ELSEVIER SCIENCE INC
- 발행년도 2018
- URI http://www.dcollection.net/handler/ewha/000000155831
- 본문언어 영어
- Published As http://dx.doi.org/10.1016/j.cellsig.2018.09.003
초록/요약
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 trans membrane 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.
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