Search Results - "Seaman, Matthew"
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The Retromer Complex: From Genesis to Revelations
Published in Trends in biochemical sciences (Amsterdam. Regular ed.) (01-07-2021)“…The retromer complex has a well-established role in endosomal protein sorting, being necessary for maintaining the dynamic localisation of hundreds of membrane…”
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The retromer complex - endosomal protein recycling and beyond
Published in Journal of cell science (15-10-2012)“…The retromer complex is a vital element of the endosomal protein sorting machinery that is conserved across all eukaryotes. Retromer is most closely associated…”
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Mutation in VPS35 associated with Parkinson’s disease impairs WASH complex association and inhibits autophagy
Published in Nature communications (13-05-2014)“…Endosomal protein sorting controls the localization of many physiologically important proteins and is linked to several neurodegenerative diseases. VPS35 is a…”
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Retromer-mediated endosomal protein sorting: all WASHed up
Published in Trends in cell biology (01-11-2013)“…Highlights • Localised actin patches on endosomes define discrete domains to facilitate protein sorting. • Formation of branched actin on endosomes requires…”
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Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
Published in Journal of cell science (15-07-2009)“…Retromer is a membrane-associated heteropentameric coat complex that functions in the endosome-to-Golgi retrieval of the cation-independent mannose-6-phosphate…”
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The fifth adaptor protein complex
Published in PLoS biology (01-10-2011)“…Adaptor protein (AP) complexes sort cargo into vesicles for transport from one membrane compartment of the cell to another. Four distinct AP complexes have…”
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Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval
Published in Journal of cell science (15-07-2007)“…The cation-independent mannose 6-phosphate receptor (CIMPR) cycles between the trans-Golgi network (TGN) and endosomes to mediate sorting of lysosomal…”
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Loss of ARPC1B impairs cytotoxic T lymphocyte maintenance and cytolytic activity
Published in The Journal of clinical investigation (01-12-2019)“…CD8 cytotoxic T lymphocytes (CTLs) rely on rapid reorganization of the branched F-actin network to drive the polarized secretion of lytic granules, initiating…”
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A dimmer switch for endosome-to-cell surface recycling
Published in The Journal of cell biology (05-04-2021)“…Endosome-to-cell surface recycling is mediated by retromer and Snx27. In this issue, Mao et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202010048)…”
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Identification of Alzheimer disease-associated variants in genes that regulate retromer function
Published in Neurobiology of aging (01-09-2012)“…Abstract The proteolytic processing of amyloid precursor protein (APP) to generate the neurotoxic amyloid β (Aβ) peptide is central to the pathogenesis of…”
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An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome
Published in The Journal of cell biology (05-08-2013)“…Mechanisms coordinating endosomal degradation and recycling are poorly understood, as are the cellular roles of microtubule (MT) severing. We show that cells…”
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Recruitment of the endosomal WASH complex is mediated by the extended 'tail' of Fam21 binding to the retromer protein Vps35
Published in Biochemical journal (15-02-2012)“…The retromer complex is a conserved endosomal protein sorting complex that sorts membrane proteins into nascent endosomal tubules. The recognition of membrane…”
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Retromer and the cation‐independent mannose 6‐phosphate receptor—Time for a trial separation?
Published in Traffic (Copenhagen, Denmark) (01-02-2018)“…The retromer cargo‐selective complex (CSC) comprising Vps35, Vps29 and Vps26 mediates the endosome‐to‐Golgi retrieval of the cation‐independent mannose…”
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cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics
Published in Journal of cell science (01-11-2010)“…The retromer complex is required for the efficient endosome-to-Golgi retrieval of the CIMPR, sortilin, SORL1, wntless and other physiologically important…”
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A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
Published in The Journal of cell biology (02-09-2019)“…Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome…”
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RME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation
Published in Journal of cell science (01-05-2014)“…Retromer is a vital element of the endosomal protein sorting machinery and comprises two subcomplexes that operate together to sort membrane proteins (cargo)…”
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Cargo-Selective Endosomal Sorting for Retrieval to the Golgi Requires Retromer
Published in The Journal of cell biology (12-04-2004)“…Efndosome-to-Golgi retrieval of the mannose 6-phosphate receptor (MPR) is required for lysosome biogenesis. Currently, this pathway is poorly understood…”
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Inhibition of TBC1D5 activates Rab7a and can enhance the function of the retromer cargo-selective complex
Published in Journal of cell science (15-06-2018)“…The retromer complex is a vital component of the endosomal protein sorting machinery necessary for sorting into both the endosome-to-Golgi retrieval pathway…”
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Myosin VI and its interacting protein LMTK2 regulate tubule formation and transport to the endocytic recycling compartment
Published in Journal of cell science (15-12-2007)“…Myosin VI is an actin-based retrograde motor protein that plays a crucial role in both endocytic and secretory membrane trafficking pathways. Myosin VI's…”
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Back From the Brink: Retrieval of Membrane Proteins From Terminal Compartments: Unexpected Pathways for Membrane Protein Retrieval From Vacuoles and Endolysosomes
Published in BioEssays (01-03-2019)“…It has long been believed that membrane proteins present in degradative compartments such as endolysosomes or vacuoles would be destined for destruction. Now…”
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