Regulation of actin-based cell migration by cAMP/PKA

Biochim Biophys Acta. 2004 Jul 5;1692(2-3):159-74. doi: 10.1016/j.bbamcr.2004.03.005.


A wide variety of soluble signaling substances utilize the cyclic AMP-dependent protein kinase (PKA) pathway to regulate cellular behaviors including intermediary metabolism, ion channel conductivity, and transcription. A growing literature suggests that integrin-mediated cell adhesion may also utilize PKA to modulate adhesion-associated events such as actin cytoskeletal dynamics and migration. PKA is dynamically regulated by integrin-mediated cell adhesion to extracellular matrix (ECM). Furthermore, while some hallmarks of cell migration and cytoskeletal organization require PKA activity (e.g. activation of Rac and Cdc42; actin filament assembly), others are inhibited by it (e.g. activation of Rho and PAK; interaction of VASP with the c-Abl tyrosine kinase). Also, cell migration and invasion can be impeded by either inhibition or hyper-activation of PKA. Finally, a number of A-kinase anchoring proteins (AKAPs) serve to associate PKA with various components of the actin cytoskeleton, thereby enhancing and/or specifying cAMP/PKA signaling in those regions. This review discusses the growing literature that supports the hypothesis that PKA plays a central role in cytoskeletal regulation and cell migration.

Publication types

  • Review

MeSH terms

  • Actin Cytoskeleton / physiology*
  • Actins / metabolism
  • Animals
  • Cell Adhesion / physiology*
  • Cell Movement / physiology*
  • Cyclic AMP-Dependent Protein Kinases / physiology*
  • Cytoskeleton / physiology*
  • Humans
  • Signal Transduction


  • Actins
  • Cyclic AMP-Dependent Protein Kinases