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    Actin polymerization is stimulated by actin cross-linking protein palladin

    Date
    2016-02-09
    Author
    Gurung, Ritu
    Yadav, Rahul
    Brungardt, Joseph G.
    Orlova, Albina
    Egelman, Edward H.
    Beck, Moriah R.
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    Citation
    Ritu Gurung, Rahul Yadav, Joseph G. Brungardt, Albina Orlova, Edward H. Egelman, Moriah R. Beck. Actin polymerization is stimulated by actin cross-linking protein palladin. Biochemical Journal, Feb 2016, 473 (4) 383-396
    Abstract
    The actin scaffold protein palladin regulates both normal cell migration and invasive cell motility, processes that require the co-ordinated regulation of actin dynamics. However, the potential effect of palladin on actin dynamics has remained elusive. In the present study, we show that the actin-binding immunoglobulin-like domain of palladin, which is directly responsible for both actin binding and bundling, also stimulates actin polymerization in vitro. Palladin eliminated the lag phase that is characteristic of the slow nucleation step of actin polymerization. Furthermore, palladin dramatically reduced depolymerization, slightly enhanced the elongation rate, and did not alter the critical concentration. Microscopy and in vitro crosslinking assays reveal differences in actin bundle architecture when palladin is incubated with actin before or after polymerization. These results suggest a model whereby palladin stimulates a polymerization-competent form of globular or monomeric actin (G-actin), akin to metal ions, either through charge neutralization or through conformational changes.
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    URI
    http://dx.doi.org/10.1042/BJ20151050
    http://hdl.handle.net/10057/12071
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