Intracellular transport mechanisms of signal transducers

Gerald W. Dorn, Daria Mochly-Rosen

Research output: Contribution to journalReview article

125 Scopus citations

Abstract

Recent discoveries have revolutionized our conceptions of enzyme-substrate specificity in signal transduction pathways. Protein kinases A and C are localized to discreet subcellular regions, and this localization changes in an isozyme-specific manner upon activation, a process referred to as translocation. The mechanisms for translocation involve interactions of soluble kinases with membrane-bound anchor proteins that recognize individual kinase isoenzymes and their state of activation. Recently, modulation of kinase-anchor protein interactions has been used to specifically regulate, positively or negatively, the activity of C kinase isozymes. Also described in this review is a role for the Rab family of small G proteins in regulating subcellular protein trafficking. The pathophysiological significance of disrupted subcellular protein transport in cell signaling and the potential therapeutic utility of targeted regulation of these events are in the process of being characterized.

Original languageEnglish
Pages (from-to)407-429
Number of pages23
JournalAnnual Review of Physiology
Volume64
DOIs
StatePublished - Apr 9 2002
Externally publishedYes

Keywords

  • Anchoring proteins
  • Protein kinase A
  • Protein kinase C
  • Rab GTPase
  • Translocation

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