Results 41 to 50 of about 7,439,285 (173)
Structural characterisation of retromer complexes [PDF]
Acta Crystallographica Section A Foundations and Advances, 2014 Retromer is a peripheral membrane protein complex that plays a critical role in a broad range of physiological, developmental and pathological processes including Wnt signalling, toxin transport and amyloid production in Alzheimer's disease. The classical mammalian retromer complex consists of a core heterotrimeric cargo recognition sub-complex (VPS26,
Suzanne Norwood +6 more
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Functional architecture of the retromer cargo-recognition complex [PDF]
Nature, 2007 The retromer complex is required for the sorting of acid hydrolases to lysosomes, transcytosis of the polymeric immunoglobulin receptor, Wnt gradient formation, iron transporter recycling and processing of the amyloid precursor protein.
Aitor, Hierro +8 more
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Mistargeting of secretory cargo in retromer-deficient cells
Disease Models & Mechanisms, 2021 Intracellular trafficking is a basic and essential cellular function required for delivery of proteins to the appropriate subcellular destination; this process is especially demanding in professional secretory cells, which synthesize and secrete massive ...
Sarah D. Neuman +4 more
doaj +1 more source
The retromer complex regulates C. elegans development and mammalian ciliogenesis.
J Cell Sci, 2022 ABSTRACT The mammalian retromer consists of subunits VPS26 (either VPS26A or VPS26B), VPS29 and VPS35, and a loosely associated sorting nexin (SNX) heterodimer or a variety of other SNX proteins. Despite involvement in yeast and mammalian cell trafficking, the role of retromer in development is poorly understood, and its impact on ...
Xie S +9 more
europepmc +3 more sources
SORLA‐retromer complex formation rely on receptor dimerization within the endosome
Alzheimer's & Dementia, 2023 SORLA acts as an endosome recycling receptor together with the retromer complex to escort cargo through the endo‐lysosomal tubular network. SORLA is encoded by the SORL1 gene, which is the gene most frequently mutated in patients with Alzheimer’s disease,
Olav M. Andersen
semanticscholar +1 more source
Cellular Logistics, 2012 Retrograde trafficking mediates the transport of endocytic membranes from endosomes to the trans-Golgi network (TGN). Dysregulation of these pathways can result in multiple ailments, including late-onset Alzheimer disease. One of the key retrograde transport regulators, the retromer complex, is tightly controlled by many factors, including the C ...
Zhang, Jing +2 more
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Direct binding of retromer to human papillomavirus type 16 minor capsid protein L2 mediates endosome exit during viral infection. [PDF]
PLoS Pathogens, 2015 Trafficking of human papillomaviruses to the Golgi apparatus during virus entry requires retromer, an endosomal coat protein complex that mediates the vesicular transport of cellular transmembrane proteins from the endosome to the Golgi apparatus or the ...
Andreea Popa +8 more
doaj +1 more source
Vps26A and Vps26B Subunits Define Distinct Retromer Complexes [PDF]
Traffic, 2011 The trimeric Vps29–Vps35–Vps26 sub‐complex of retromer mediates retrograde transport of transmembrane proteins from endosomes to the trans‐Golgi network. Our group has recently identified a Vps26 paralogue, Vps26B, which is able to suppress the expression of Vps26A when exogenously expressed in mammalian cells and defines a distinct retromer complex ...
Bugarcic, Andrea +5 more
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Retromer deficiency in Tauopathy models enhances the truncation and toxicity of Tau
Nature Communications, 2022 Tau and the Retromer complex are both linked to Parkinson’s and Alzheimer’s disease. Using Drosophila neurodegeneration models, this study finds that low retromer activity induces a specific increase of a highly toxic truncated form of human Tau.
Jamshid Asadzadeh +8 more
doaj +1 more source
A FAM21-Containing WASH Complex Regulates Retromer-Dependent Sorting [PDF]
Developmental Cell, 2009 The Arp2/3 complex regulates endocytosis, sorting, and trafficking, yet the Arp2/3-stimulating factors orchestrating these distinct events remain ill defined. WASH (Wiskott-Aldrich Syndrome Protein and SCAR Homolog) is an Arp2/3 activator with unknown function that was duplicated during primate evolution.
Gomez, Timothy S., Billadeau, Daniel D.
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