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- W2901357662 endingPage "1604" @default.
- W2901357662 startingPage "1587" @default.
- W2901357662 abstract "Actin filament assembly typically occurs in association with cellular membranes. A large number of proteins sit at the interface between actin networks and membranes, playing diverse roles such as initiation of actin polymerization, modulation of membrane curvature, and signaling. Bin/Amphiphysin/Rvs (BAR) domain proteins have been implicated in all of these functions. The BAR domain family of proteins comprises a diverse group of multi-functional effectors, characterized by their modular architecture. In addition to the membrane-curvature sensing/inducing BAR domain module, which also mediates antiparallel dimerization, most contain auxiliary domains implicated in protein-protein and/or protein-membrane interactions, including SH3, PX, PH, RhoGEF, and RhoGAP domains. The shape of the BAR domain itself varies, resulting in three major subfamilies: the classical crescent-shaped BAR, the more extended and less curved F-BAR, and the inverse curvature I-BAR subfamilies. Most members of this family have been implicated in cellular functions that require dynamic remodeling of the actin cytoskeleton, such as endocytosis, organelle trafficking, cell motility, and T-tubule biogenesis in muscle cells. Here, we review the structure and function of mammalian BAR domain proteins and the many ways in which they are interconnected with the actin cytoskeleton." @default.
- W2901357662 created "2018-11-29" @default.
- W2901357662 creator A5063558144 @default.
- W2901357662 creator A5078781578 @default.
- W2901357662 date "2018-11-19" @default.
- W2901357662 modified "2023-10-17" @default.
- W2901357662 title "BAR domain proteins—a linkage between cellular membranes, signaling pathways, and the actin cytoskeleton" @default.
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