Structure and function of palladin's actin binding domain
| Autor: | Moriah R. Beck, Pavan Srinath, Grant S. Murphy, Jahan J. Mohiuddin, Joseph G. Brungardt, Richard D.S. Dixon, Matthew T. Beam, Sharon L. Campbell, Carol A. Otey, Julie B. Patel, Silvia M. Goicoechea |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Arp2/3 complex Immunoglobulins macromolecular substances Filamin Transfection Filamentous actin Article Actin remodeling of neurons Mice Structural Biology Chlorocebus aethiops Protein Interaction Mapping Animals Protein Interaction Domains and Motifs Actin-binding protein Cytoskeleton Molecular Biology biology Palladin Actin remodeling Phosphoproteins Actins Cell biology Cytoskeletal Proteins Protein Transport Amino Acid Substitution COS Cells biology.protein Mutagenesis Site-Directed Rabbits Protein Binding |
| Zdroj: | Journal of molecular biology. 425(18) |
| ISSN: | 1089-8638 |
| Popis: | 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 filamentous actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and cross-linking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin cross-linking 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. |
| Databáze: | OpenAIRE |
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