TAILIEUCHUNG - Báo cáo khoa học: Vps4 regulates a subset of protein interactions at the multivesicular endosome

During endocytic transport, specific integral membrane proteins are sorted into intraluminal vesicles that bud from the limiting membrane of the endosome. This process, known as multivesicular body (MVB) sorting, is important for several important biological processes. | ễFEBS Journal Vps4 regulates a subset of protein interactions at the multivesicular endosome Parimala R. Vajjhala1 Elizabeth Catchpoole1 Chau H. Nguyen1 Carol Kistler1 and Alan L. Munn1 2 1 Institute for Molecular Bioscience and ARC SpecialResearch Centre for Functionaland Applied Genomics University of Queensland St Lucia QLD Australia 2 Schoolof BiomedicalSciences University of Queensland St Lucia QLD Australia Keywords endocytosis lysosome macromolecular disassembly membrane traffic vacuole Correspondence A. L. Munn Institute for Molecular Bioscience University of Queensland St Lucia Brisbane QLD 4072 Australia Fax 61 73346 2101 Tel 61 73346 2017 E-mail Received 17 December 2006 revised 6 February 2007 accepted 9 February 2007 doi During endocytic transport specific integral membrane proteins are sorted into intraluminal vesicles that bud from the limiting membrane of the endosome. This process known as multivesicular body MVB sorting is important for several important biological processes. Moreover components of the MVB sorting machinery are implicated in virus budding. During MVB sorting a cargo protein recruits components of the MVB sorting machinery from cytoplasmic pools and these sequentially assemble on the endosome. Disassembly of these proteins and recycling into the cytoplasm is critical for MVB sorting. Vacuolar protein sorting 4 Vps4 is an AAA ATPase associated with a variety of cellular activities ATPase which has been proposed to play a critical role in disassembly of the MVB sorting machinery. However the mechanism by which it disassembles the complex is not clear. Vps4 contains an N-terminal microtubule interacting and trafficking MIT domain which has previously been shown to be required for recruitment to endosomes and a single AAA ATPase domain the activity of which is required for Vps4 function. In this study we have systematically characterized the interaction of Vps4 with other components

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