Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation

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    272 Citations (Scopus)


    Cofilin and actin-depolymerizing factor (ADF) are actin-binding proteins that play an essential role in regulating actin filament dynamics and reorganization by stimulating the severance and depolymerization of actin filaments. Cofilin/ADF are inactivated by phosphorylation at the serine residue at position 3 by LIM-kinases (LIMKs) and testicular protein kinases (TESKs) and are reactivated by dephosphorylation by the slingshot (SSH) family of protein phosphatases and chronophin. This review describes recent advances in our understanding of the signaling mechanisms regulating LIMKs and SSHs and the functional roles of cofilin phospho-regulation in cell migration, tumor invasion, mitosis, neuronal development, and synaptic plasticity. Accumulating evidence demonstrates that the phospho-regulation of cofilin/ADF is a key convergence point of cell signaling networks that link extracellular stimuli to actin cytoskeletal dynamics and that spatiotemporal control of cofilin/ADF activity by LIMKs and SSHs plays a crucial role in a diverse array of cellular and physiological processes. Perturbations in the normal control of cofilin/ADF activity underlie many pathological conditions, including cancer metastasis and neurological and cardiovascular disorders.

    Original languageEnglish
    Pages (from-to)457-469
    Number of pages13
    JournalCellular Signalling
    Issue number2
    Publication statusPublished - 2013 Feb


    • Cancer invasion
    • Cell migration
    • Cofilin
    • LIM kinase
    • Neuronal development
    • Slingshot

    ASJC Scopus subject areas

    • Cell Biology


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