Identification of a clathrin binding subunit in the HA2 adaptor protein complex
نویسندگان
چکیده
منابع مشابه
A membrane-associated protein complex with selective binding to the clathrin coat adaptor AP1.
Adaptors are the membrane-binding components of clathrin-coated vesicles. The interaction of the trans-Golgi coat adaptor AP1 with membrane-associated proteins was analyzed by affinity chromatography. Proteins of 83 and 52 kDa bound specifically to the core domain of AP1 and showed no interaction with AP2 or other clathrin-coated vesicle proteins. The AP1-binding proteins were tightly membrane-...
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The heterotetrameric AP-1 adaptor complex is involved in the assembly of clathrin-coated vesicles originating from the trans-Golgi network (TGN). The beta 1 subunit of AP-1 is known to contain a consensus clathrin binding sequence, LLNLD (the so-called clathrin box motif), in its hinge segment through which the beta chain interacts with the N-terminal domains of clathrin trimers. Here, we repor...
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Clathrin-associated adaptor protein (AP) complexes are major structural components of clathrin-coated vesicles, functioning in clathrin coat assembly and cargo selection. We have carried out a systematic biochemical and genetic characterization of AP complexes in Saccharomyces cerevisiae. Using coimmunoprecipitation, the subunit composition of two complexes, AP-1 and AP-2R, has been defined. Th...
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Membrane traffic among organelles of the secretory and endocytic pathways is mediated by small, transport vesicles that are classified according to the protein coat used in their formation and the cargo they contain (Bonifacino and Glick, 2004; Bonifacino and LippincottSchwartz, 2003). Clathrin-coated vesicles (CCVs) are involved in the transport between organelles, such as the trans-Golgi netw...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)47222-0