Building endocytic pits without clathrin.
Paris, France. In Nat Rev Mol Cell Biol, May 2015
Recent insight suggests that different forms of clathrin-independent endocytosis might involve the actin-driven focusing of membrane constituents, the lectin-glycosphingolipid-dependent construction of endocytic nanoenvironments, and Bin-Amphiphysin-Rvs (BAR) domain proteins serving as scaffolding modules.
Membrane-associated cargo recycling by tubule-based endosomal sorting.
Amsterdam, Netherlands. In Semin Cell Dev Biol, 2014
These tubules are formed and stabilized through the scaffolding properties of cytosolic Bin/Amphiphysin/Rvs (BAR) proteins that comprise phosphoinositide-detecting moieties, recruiting these proteins to specific endosomal membrane areas.
BAR domain proteins regulate Rho GTPase signaling.
Stockholm, Sweden. In Small Gtpases, 2013
The common denominator is the Bin-Amphiphysin-Rvs (BAR) domain that not only confers targeting to lipid bilayers, but also provides scaffolding to mold lipid membranes into concave or convex surfaces.
AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling.
United States. In Nat Cell Biol, 2009
Here we show that endogenous C. elegans AMPH-1, the only C. elegans member of the Amphiphysin/BIN1 family of BAR (Bin1-Amphiphysin-Rvs161p/167p)-domain-containing proteins, colocalizes with RME-1 on recycling endosomes in vivo, that amph-1-deletion mutants are defective in recycling endosome morphology and function, and that binding of AMPH-1 Asn-Pro-Phe(Asp/Glu) sequences to the RME-1 EH-domain promotes the recycling of transmembrane cargo.