A role for the hinge/ear domain of the beta chains in the incorporation of AP complexes into clathrin-coated pits and coated vesicles.
The clathrin-associated adaptor protein (AP) complexes drive the polymerization of clathrin in coated pits to form coated vesicles. It has previously been shown that the carboxyl-terminal hinge/ear domain of the beta 2 chain contains a binding site for clathrin and that removal of this domain from APs or from isolated beta 2 chains abrogates their ability to form clathrin coats in vitro. We show here that the hinge/ear domain is necessary for efficient incorporation of AP complexes into coated pits and coated vesicles in cells, a result that is consistent with the view that the beta chains indeed provide an important interaction between the AP complexes and clathrin.
Clairmont
K B
KB
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Boll
W
W
Ericsson
M
M
Kirchhausen
T
T
D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D015153:Blotting, Western; D016466:CHO Cells; D002462:Cell Membrane / Q000648:ultrastructure; D002966:Clathrin / Q000378:metabolism*; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism*; D018699:Coated Vesicles / Q000378:metabolism*; D006224:Cricetinae; D018076:DNA, Complementary / Q000235:genetics; D004705:Endocytosis; D000939:Epitopes / Q000276:immunology; D006056:Golgi Apparatus / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014162:Transfection
D033942:Adaptor Proteins, Vesicular Transport; D002966:Clathrin; D018076:DNA, Complementary; D000939:Epitopes; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D011994:Recombinant Proteins