Ever-Expanding Network of Dynamin-Interacting Proteins

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Abstract
Clathrin-mediated endocytosis is a major cellular pathway for internalization of proteins and lipids and for recycling of synaptic vesicles. The GTPase dynamin plays a key role in this process, and the proline-rich domain of dynamin participates in various protein-protein interactions to ensure a proper coordination of endocytic processes. Although dynamin is not directly associated with actin, several dynamin-binding proteins can interact with actin or with proteins that regulate actin assembly, thereby coordinately regulating actin assembly and trafficking events. This article summarizes dynamin interactions with various Src homology 3-containing proteins, many of which are actin-binding proteins. It also discusses the recently identified two new dynamin binding proteins, SH3 protein interacting with Nck, 90 kDa/Wiskott-Aldrich syndrome protein interacting with SH3 protein (SPIN90/WISH) and sorting nexin 9, and outlines their potential role as a link between endocytosis and actin dynamics.