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Updated: May 12, 2026

In Vitro Polymerization of F-actin on Early Endosomes
Published on: August 28, 2017
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin
K E Prehoda1, D J Lee, W A Lim
1Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA.
Abstract:
The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an interaction module found in several proteins implicated in actin-based cell motility. EVH1 domains bind the consensus proline-rich motif FPPPP and are required for targeting the actin assembly machinery to sites of cytoskeletal remodeling. The crystal structure of the mammalian Enabled (Mena) EVH1 domain complexed with a peptide ligand reveals a mechanism of recognition distinct from that used by other proline-binding modules. The EVH1 domain fold is unexpectedly similar to that of the pleckstrin homology domain, a membrane localization module. This finding demonstrates the functional plasticity of the pleckstrin homology fold as a binding scaffold and suggests that membrane association may play an auxiliary role in EVH1 targeting.
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