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Proteomic analysis of clathrin‐coated vesicles
Author(s) -
McPherson Peter S.
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000253
Subject(s) - clathrin , organelle , proteomics , endocytic cycle , microbiology and biotechnology , golgi apparatus , clathrin adaptor proteins , endosome , vesicle , biology , vesicular transport protein , function (biology) , secretory pathway , copi , chemistry , endocytosis , cell , biochemistry , endoplasmic reticulum , membrane , gene , intracellular
For more than 50 years cell biologists have embraced the concept that biochemical and enzymatic analysis of isolated subcellular fractions provides insight into the function and machineries of cellular compartments including organelles. The utility of this approach has been significantly enhanced with the advent of mass spectrometry leading to the broad application of organelle proteomics. Clathrin‐coated vesicles (CCVs) form at the plasma membrane where they select protein and lipid cargo for endocytic entry into cells. CCVs also form at the trans‐Golgi network, where they function in protein transport from the secretory pathway to the endosomal/lysosomal system. Herein we will describe how organelle proteomics of CCVs has greatly expanded our knowledge of the machineries, mechanisms and sites of clathrin‐mediated membrane trafficking.