Structural mechanisms of plexin signaling

Heath G. Pascoe, Yuxiao Wang, Xuewu Zhang

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Signaling through plexin, the major cell surface receptor for semaphorin, plays critical roles in regulating processes such as neuronal axon guidance, angiogenesis and immune response. Plexin is normally kept inactive in the absence of semaphorin. Upon binding of semaphorin to the extracellular region, plexin is activated and transduces signal to the inside of the cell through its cytoplasmic region. The GTPase Activating Protein (GAP) domain in the plexin cytoplasmic region mediates the major intracellular signaling pathway. The substrate specificity and regulation mechanisms of the GAP domain have only been revealed recently. Many intracellular proteins serve as either upstream regulators or downstream transducers by directly interacting with plexin. The mechanisms of action for some of these proteins also start to emerge from recent studies. We review here these advances in the mechanistic understanding of plexin intracellular signaling from a structural perspective.

Original languageEnglish (US)
Pages (from-to)161-168
Number of pages8
JournalProgress in Biophysics and Molecular Biology
Volume118
Issue number3
DOIs
StatePublished - Sep 1 2015

Keywords

  • Dimerization
  • GAP
  • Plexin
  • Rap
  • Signaling

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics

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