A role for the hinge/ear domain of the β chains in the incorporation of AP complexes into clathrin-coated pits and coated vesicles |
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Authors: | K B Clairmont W Boll M Ericsson T Kirchhausen |
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Institution: | (1) Department of Cell Biology, Harvard Medical School and Center for Blood Research, 200 Longwood Ave., Boston (Massachusetts 02115, USA), Fax +1 617 278 3131, e-mail: kirchhausen@xtal0.harvard.edu, US |
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Abstract: | 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 β2 chain contains a binding site for clathrin and that removal of this domain from APs or from isolated β2 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 β chains indeed provide an important interaction between the AP complexes and clathrin.
Received 7 April 1997; received after revision 22 May 1997; accepted 28 May 1997 |
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Keywords: | , Coated pits, vesicles, endocytosis, adaptors, coat assembly, |
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