Structure and function of palladin’s actin binding domain
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.
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.
Other Names
Location
Time Period
Advisors
Original Date
Digitization Date
Issue Date
2013-06-25
Type
Preprint
Genre
Keywords
Subjects (LCSH)
Citation
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.
Table of Contents
Description
Click on the DOI link to access the article (may not be free).
Publisher
Elsevier
Journal
Book Title
Series
Journal of Molecular Biology;
Digital Collection
Finding Aid URL
Use and Reproduction
Archival Collection
PubMed ID
DOI
ISSN
0022-2836