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Recognition of sorting signals by clathrin adaptors
Author(s) -
Heilker Ralf,
Spiess Martin,
Crottet Pascal
Publication year - 1999
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199907)21:7<558::aid-bies4>3.0.co;2-r
Subject(s) - clathrin , endosome , clathrin adaptor proteins , microbiology and biotechnology , internalization , endocytosis , protein targeting , protein sorting signals , signal transducing adaptor protein , sorting , golgi apparatus , biology , vesicle , membrane protein , receptor , membrane , signal transduction , biochemistry , signal peptide , peptide sequence , computer science , gene , endoplasmic reticulum , intracellular , programming language
Sorting of membrane proteins is generally mediated by cytosolic coats, which create a scaffold to form coated buds and vesicles and to selectively concentrate cargo by interacting with cytosolic signals. The classical paradigm is the interaction between clathrin coats and associated adaptor proteins, which cluster receptors with characteristic tyrosine and dileucine motifs during endocytosis. Clathrin in association with different sets of adaptors is found in addition at the trans ‐Golgi network and endosomes. Sequences similar to internalization signals also direct lysosomal and basolateral sorting, which implicates related clathrin‐adaptor coats in the respective sorting pathways. This review concentrates on the recognition of sorting signals by clathrin‐associated adaptor proteins, an area of significant recent progress due to new methodological and conceptual approaches. BioEssays 21:558–567, 1999. © 1999 John Wiley & Sons, Inc.