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Kirsty J McMillan, Matthew Gallon, Adam P Jellett, Thomas Clairfeuille, Frances C Tilley, Ian McGough, Chris M Danson, Kate J Heesom, Kevin A Wilkinson, Brett M Collins, Peter J Cullen
The retromer complex acts as a scaffold for endosomal protein complexes that sort integral membrane proteins to various cellular destinations. The retromer complex is a heterotrimer of VPS29, VPS35, and VPS26. Two of these paralogues, VPS26A and VPS26B, are expressed in humans. Retromer dysfunction is associated with neurodegenerative disease, and recently, three VPS26A mutations (p.K93E, p.M112V, and p.K297X) were discovered to be associated with atypical parkinsonism. Here, we apply quantitative proteomics to provide a detailed description of the retromer interactome...
August 15, 2016: Journal of Cell Biology
Andrea Bugarcic, Irina Vetter, Silke Chalmers, Genevieve Kinna, Brett M Collins, Rohan D Teasdale
Retromer is a trimeric complex composed of Vps26, Vps29, and Vps35 and has been shown to be involved in trafficking and sorting of transmembrane proteins within the endosome. The Vps26 paralog, Vps26B, defines a distinct retromer complex (Vps26B-retromer) in vivo and in vitro. Although endosomally associated, Vps26B-retromer does not bind the established retromer transmembrane cargo protein, cation-independent mannose 6-phosphate receptor (CI-M6PR), indicating it has a distinct role to retromer containing the Vps26A paralog...
November 2015: Cell Biology International
Emil K Gustavsson, Ilaria Guella, Joanne Trinh, Chelsea Szu-Tu, Alex Rajput, Ali H Rajput, John C Steele, Martin McKeown, Beom S Jeon, Jan O Aasly, Matthew J Farrer
BACKGROUND: A pathogenic mutation (VPS35 p.D620N) within the retromer complex has been shown to segregate with late-onset Parkinson's disease (PD). Several studies have subsequently detected the mutation in patients with PD and not in controls. METHODS: Mutation screening of the coding regions of the retromer cargo recognition complex genes (VPS26A/B, VPS29, and VPS35) was carried out in patients with PD (n = 396), atypical parkinsonism (n = 229), and in 368 controls...
April 2015: Movement Disorders: Official Journal of the Movement Disorder Society
Trinidad Montero-Meléndez, Xavier Llor, Esther García-Planella, Mauro Perretti, Antonio Suárez
BACKGROUND: Improvement of patient quality of life is the ultimate goal of biomedical research, particularly when dealing with complex, chronic and debilitating conditions such as inflammatory bowel disease (IBD). This is largely dependent on receiving an accurate and rapid diagnose, an effective treatment and in the prediction and prevention of side effects and complications. The low sensitivity and specificity of current markers burden their general use in the clinical practice. New biomarkers with accurate predictive ability are needed to achieve a personalized approach that take the inter-individual differences into consideration...
2013: PloS One
Andrea Bugarcic, Yang Zhe, Markus C Kerr, John Griffin, Brett M Collins, Rohan D Teasdale
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 (Vps26B-retromer) in vivo and in vitro. In this study, we use HEK293 cells stably expressing either Vps26A-myc or Vps26B-myc to address the role of retromer cargo transport and subcellular localization of the two core retromer complexes as defined by the two mammalian-specific Vps26 paralogues...
December 2011: Traffic
Sang-Je Park, Jae-Won Huh, Young-Hyun Kim, Ji-Su Kim, Bong-Seok Song, Sang-Rae Lee, Sun-Uk Kim, Heui-Soo Kim, Kazuhiko Imakawa, Kyu-Tae Chang
The retromer complex is a heteropentameric protein unit associated with retrograde transport of cargo proteins from endosomes to the trans-Golgi network. Functional silencing study of the Vps26a gene indicated the important role of the retromer complex during early developmental stages in the mouse. However, individual expression patterns and quantitative analysis of individual members of the retromer complex during the early developmental stages has not been investigated. In this study, we conducted quantitative expression analysis of six retromer complex genes (Vps26a, Vps26b, Vps29, Vps35, Snx1, and Snx2) and one related receptor gene (Ci-mpr) during the eleven embryonic stages with normal MEF (mouse embryonic fibroblast) and Vps26a(-/-) MEF cells...
May 2011: Molecules and Cells
Ekyune Kim, Youngjeon Lee, Hyun-Ju Lee, Ji Su Kim, Bong-Seok Song, Jae-Won Huh, Sang-Rae Lee, Sun-Uk Kim, Sang-Hyun Kim, Yonggeun Hong, Insop Shim, Kyu-Tae Chang
The retromer complex, which mediates retrograde transport from endosomes to the trans-Golgi network, is a heteropentameric complex that contains a multifunctional cargo recognition heterotrimer consisted of the vacuolar protein sorting (Vps) subunits Vps26, Vps29, and Vps35. In mammals, there are two different isoforms of Vps26, Vps26a and Vps26b, that localize to the endosome, and to the plasma membrane, respectively. To elucidate the biological significance of the Vps26b isoform, we generated Vps26b knockout mice and studied their molecular, histological, and behavioral phenotypes...
December 10, 2010: Biochemical and Biophysical Research Communications
Ekyune Kim, Jae-Woong Lee, Dong-Chul Baek, Sang-Rae Lee, Myeong-Su Kim, Sang-Hyun Kim, Kazuhiko Imakawa, Kyu-Tae Chang
A family of vacuolar protein sorting (Vps) proteins, which are components of mammalian retromer complex, has been studied in the mouse. Vps26a is known as a retromer component that plays an important role in embryonic development: however, its cell-type expression and precise role remain to be elucidated. In this study, we identified a new isoform of Vps26a, called Vps26aT, which was expressed specifically in the mouse testis. Diverse expression patterns of Vps26 variants in mouse tissues were determined by Western blot and RT-PCR analyses, and the direct interaction of Vps26aT with Vps35 was also demonstrated by immunoprecipitation and pull-down assay using antibodies raised against each Vps component...
October 10, 2008: Biochemical and Biophysical Research Communications
Brett M Collins, Suzanne J Norwood, Markus C Kerr, Donna Mahony, Matthew N J Seaman, Rohan D Teasdale, David J Owen
Retromer is a heteromeric protein complex with important roles in endosomal membrane trafficking, most notably in the retrograde transport of lysosomal hydrolase receptors from endosomes to the Golgi. The core of retromer is composed of three subunits vacuolar protein sorting (Vps)35, Vps26 and Vps29, and in mammals, there are two paralogues of the medium subunit Vps26A and Vps26B. We find that both Vps26A and Vps26B bind to Vps35/Vps29 with nanomolar affinity and compete for a single-binding site to define distinct retromer complexes in vitro and in vivo...
March 2008: Traffic
Markus C Kerr, Jennifer S Bennetts, Fiona Simpson, Elaine C Thomas, Cameron Flegg, Paul A Gleeson, Carol Wicking, Rohan D Teasdale
The mammalian retromer protein complex, which consists of three proteins--Vps26, Vps29, and Vps35--in association with members of the sorting nexin family of proteins, has been implicated in the trafficking of receptors and their ligands within the endosomal/lysosomal system of mammalian cells. A bioinformatic analysis of the mouse genome identified an additional transcribed paralog of the Vps26 retromer protein, which we termed Vps26B. No paralogs were identified for Vps29 and Vps35. Phylogenetic studies indicate that the two paralogs of Vps26 become evident after the evolution of the chordates...
November 2005: Traffic
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