You can go your own way: SNX-BAR coat complexes direct traffic at late endosomes |
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| Affiliation: | 1. Department of Medical Genetics, University of British Columbia, Vancouver, BC VH6 3N1, Canada;2. Centre for Molecular Medicine and Therapeutics, British Columbia Children''s Hospital Research Institute, University of British Columbia, Vancouver, BC V5Z 4H4, Canada;1. Student Research Committee, Mashhad University of Medical Sciences, Mashhad, Iran;2. Department of Pharmacodynamics and Toxicology, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran;3. Center for Environmental Occupational Risk Analysis and Management, College of Public Health, University of South Florida, Tampa, FL,, USA;4. Institute for Integrative Toxicology, Michigan State University, East Lansing, MI, USA;5. Pharmaceutical Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran;1. Cambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK;2. Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK;3. Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK |
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| Abstract: | The endolysosomal network consists of highly dynamic membrane-bound compartments that control subcellular degradative and recycling processes. A conserved family of endosomal coat complexes known as SNX-BARs drive the formation of tubular membrane transport carriers for cargo retrieval. Whereas SNX1-related SNX-BARs were previously thought to rely on their association with the retromer complex to recognize cargo, recent work shows this class of SNX-BARs can directly bind and deliver cargo. In this review, we examine the retromer-independent roles of SNX-BAR proteins in yeast and metazoans and explore their functional overlap with endosomal sorting complexes and accessory factors. We also discuss new work that highlights the role of the disordered N-terminal regions of SNX-BARs in complex assembly and function. |
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