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A new paradigm for membrane‐organizing and ‐shaping scaffolds
Author(s) -
Bauer Manuel,
Pelkmans Lucas
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.077
Subject(s) - copi , copii , vesicle , membrane , microbiology and biotechnology , chemistry , membrane protein , clathrin , peripheral membrane protein , caveolae , biophysics , integral membrane protein , biochemistry , golgi apparatus , biology , endoplasmic reticulum , secretory pathway
The clathrin, COPI and COPII scaffolds are paradigm vesicle coats in membrane trafficking. Recent advances in our understanding of the caveolar coat have generated a new paradigm. It represents those membrane coats, where a considerable part of the protein component is lipid modified, and integrated into the cytosolic leaflet of the vesicle membrane by a hairpin‐like hydrophobic structure. Such coat proteins are permanently associated with membranes, and form oligomers early after synthesis. These oligomers assemble into a coat that has high affinity for particular lipids, creating lipid microdomains within the membrane. The combined protein–lipid structure should be considered as the scaffold that entraps ligands, either through affinity with the protein or with the lipid component, and that has the ability to shape membranes. Besides scaffolds assembled by caveolins , scaffolds assembled by reticulons and PHB domain‐containing proteins such as the reggie/flotillin proteins fit this paradigm.