Structure and function of palladin’s actin binding domain
Date
2013-06-25Author
Beck, Moriah R.
Dixon, Richard D.S.
Goicoechea, Silvia M.
Murphy, Grant S.
Brungardt, Joseph G.
Beam, Matthew T.
Srinath, Pavan
Patel, Julie
Mohiuddin, Jahan
Otey, Carol A.
Campbell, Sharon L.
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Moriah R. Beck, Richard D.S. Dixon, Silvia M. Goicoechea, Grant S. Murphy, Joseph G. Brungardt, Matthew T. Beam, Pavan Srinath, Julie Patel, Jahan Mohiuddin, Carol A. Otey, Sharon L. Campbell, Structure and Function of Palladin’s Actin Binding Domain, Journal of Molecular Biology, Available online 25 June 2013, ISSN 0022-2836, http://dx.doi.org/10.1016/j.jmb.2013.06.016.
Abstract
Here we report the NMR structure of the actin-binding domain contained in the cell adhesion protein palladin. Previously we demonstrated that one of the immunoglobulin domains of palladin (Ig3) is both necessary and sufficient for direct F-actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and crosslinking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin crosslinking mechanism that involves concurrent attachment of two actin filaments by a single palladin molecule by an electrostatic mechanism. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo.
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