Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics

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  • Sastry, Sarita K.
    • Affiliation: N.C. Cancer Hospital, UNC Lineberger Comprehensive Cancer Center
  • Burridge, Keith
    • Affiliation: N.C. Cancer Hospital, UNC Lineberger Comprehensive Cancer Center
Abstract
  • Focal adhesions (FAs) are specialized sites of cell attachment to the extracellular matrix (ECM) where integrin receptors link the ECM to the actin cytoskeleton. Integrins cluster into supramolecular complexes with structural, cytoskeletal proteins like talin, vinculin, and a-actinin, as well as numerous signaling molecules, including c-Src, FAK, p130cas, and paxillin. The composition and molecular architecture of FAs have been reviewed elsewhere and are beyond the scope of this brief review. FAs serve at least two significant cellular functions: to transmit force or tension at adhesion sites to maintain strong attachments to the underlying ECM and to act as signaling centers from which numerous intracellular pathways emanate to regulate cell growth, survival, and gene expression. FAs are dynamic structures that assemble, disperse, and recycle (turnover) as cells migrate or enter into mitosis. Recent evidence reveals the complexity of these processes. Assembly/disassembly involves the coordinate regulation of Rho family GTPases through cross talk between integrins and numerous adhesion receptors (cadherins, cell adhesion molecules (CAMs), selectins, and syndecans), G-protein-coupled receptors (GPCRs), and receptor tyrosine kinases (RTKs), as well as the interplay between microtubules and actin. It is also apparent that FAs are themselves motile and heterogeneous in composition. Finally, turnover of FAs entails communication with components of vesicle trafficking pathways and microtubules. This review highlights recent findings relating to FA assembly, dynamics, and turnover.
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  • Journal Item
Rights statement
  • In Copyright
Journal title
  • Experimental Cell Research
Journal volume
  • 261
Journal issue
  • 1
Page start
  • 25
Page end
  • 36
Language
  • English
Version
  • Postprint
ISSN
  • 0014-4827

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