Initiation and disassembly of filopodia tip complexes containing VASP and lamellipodin
Author:
Affiliation:
1. Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143
2. Howard Hughes Medical Institute, University of California, San Francisco, CA 94143
Abstract
Publisher
American Society for Cell Biology (ASCB)
Subject
Cell Biology,Molecular Biology
Reference56 articles.
1. I-BAR domains, IRSp53 and filopodium formation
2. Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells
3. Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity
4. Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function
5. Negative Regulation of Fibroblast Motility by Ena/VASP Proteins
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