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https://www.readbyqxmd.com/read/29777037/inhibition-of-tbc1d5-activates-rab7a-and-can-enhance-the-function-of-the-retromer-cargo-selective-complex
#1
Matthew N J Seaman, Aamir S Mukadam, Sophia Y Breusegem
The retromer complex is a vital component of the endosomal protein sorting machinery being necessary for sorting into both the endosome-to-Golgi retrieval pathway and also the endosome-to-cell-surface recycling pathway. Retromer mediates cargo selection through a trimeric complex comprising VPS35, VPS29 and VPS26 which is recruited to endosomes by binding to Rab7a and Snx3. Retromer function is linked to two distinct neurodegenerative diseases, Parkinson's disease and Alzheimer's disease and modulating retromer function has been proposed as an avenue to explore for a putative therapy in these conditions...
May 18, 2018: Journal of Cell Science
https://www.readbyqxmd.com/read/29755290/retromer-dysfunction-and-neurodegenerative-disease
#2
REVIEW
Christiane Reitz
In recent years, genomic, animal and cell biology studies have implicated deficiencies in retromer-mediated trafficking of proteins in an increasing number of neurodegenerative diseases including Alzheimer's Disease (AD), Parkinson's Disease (PD) and Frontotemporal Lobar Degener-ation (FTLD). The retromer complex, which is highly conserved across all eukaryotes, regulates the sorting of transmembrane proteins out of endo-somes to the cell surface or to the trans-Golgi network. Within retromer, cargo selection and binding are performed by a trimer of the Vps26, Vps29 and Vps35 proteins, named the "Cargo-Selective Complex (CSC)"...
May 2018: Current Genomics
https://www.readbyqxmd.com/read/29678717/a-tandem-mass-tag-tmt-proteomic-analysis-during-the-early-phase-of-experimental-pancreatitis-reveals-new-insights-in-the-disease-pathogenesis
#3
Violeta García-Hernández, Carmen Sánchez-Bernal, Domitille Schvartz, José J Calvo, Jean-Charles Sanchez, Jesús Sánchez-Yagüe
Changes in the protein expression occurring within the initiation phase of acute pancreatitis (AP) might be vital in the development of this complex disease. However, the exact mechanisms involved in the onset of AP remains elusive and most of our knowledge about the pathobiology of AP comes from animal models. We performed in a rat pancreatitic model a high-throughput shotgun proteomic profiling of the soluble and whole membrane fractions from the pancreas during the early phase of cerulein (Cer)-induced AP...
April 17, 2018: Journal of Proteomics
https://www.readbyqxmd.com/read/29668757/actin-polymerization-in-the-endosomal-pathway-but-not-on-the-coxiella-containing-vacuole-is-essential-for-pathogen-growth
#4
Heather E Miller, Charles L Larson, Robert A Heinzen
Coxiella burnetii is an intracellular bacterium that replicates within an expansive phagolysosome-like vacuole. Fusion between the Coxiella-containing vacuole (CCV) and late endosomes/multivesicular bodies requires Rab7, the HOPS tethering complex, and SNARE proteins, with actin also speculated to play a role. Here, we investigated the importance of actin in CCV fusion. Filamentous actin patches formed around the CCV membrane that were preferred sites of vesicular fusion. Accordingly, the mediators of endolysosomal fusion Rab7, VAMP7, and syntaxin 8 were concentrated in CCV actin patches...
April 18, 2018: PLoS Pathogens
https://www.readbyqxmd.com/read/29495075/vacuolar-protein-sorting-26c-encodes-an-evolutionarily-conserved-large-retromer-subunit-in-eukaryotes-that-is-important-for-root-hair-growth-in-arabidopsis-thaliana
#5
Suryatapa Ghosh Jha, Emily R Larson, Jordan Humble, David S Domozych, David S Barrington, Mary L Tierney
The large retromer complex participates in diverse endosomal trafficking pathways and is essential for plant developmental programs, including cell polarity, programmed cell death and shoot gravitropism in Arabidopsis. Here we demonstrate that an evolutionarily conserved VPS26 protein (VPS26C; At1G48550) functions in a complex with VPS35A and VPS29 necessary for root hair growth in Arabidopsis. Bimolecular fluorescence complementation showed that VPS26C forms a complex with VPS35A in the presence of VPS29, and this is supported by genetic studies showing that vps29 and vps35a mutants exhibit altered root hair growth...
May 2018: Plant Journal: for Cell and Molecular Biology
https://www.readbyqxmd.com/read/29386389/mechanism-of-inhibition-of-retromer-transport-by-the-bacterial-effector-ridl
#6
Jialin Yao, Fan Yang, Xiaodong Sun, Shen Wang, Ninghai Gan, Qi Liu, Dingdong Liu, Xia Zhang, Dawen Niu, Yuquan Wei, Cong Ma, Zhao-Qing Luo, Qingxiang Sun, Da Jia
Retrograde vesicle trafficking pathways are responsible for returning membrane-associated components from endosomes to the Golgi apparatus and the endoplasmic reticulum (ER), and they are critical for maintaining organelle identity, lipid homeostasis, and many other cellular functions. The retrograde transport pathway has emerged as an important target for intravacuolar bacterial pathogens. The opportunistic pathogen Legionella pneumophila exploits both the secretory and recycling branches of the vesicle transport pathway for intracellular bacterial proliferation...
February 13, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29321327/human-papillomavirus-16-infection-induces-vap-dependent-endosomal-tubulation
#7
Abida Siddiqa, Paola Massimi, David Pim, Justyna Broniarczyk, Lawrence Banks
Human papillomavirus (HPV) infection involves complex interactions with the endocytic transport machinery, which ultimately facilitates the entry of the incoming viral genomes into the trans -Golgi network (TGN) and their subsequent nuclear entry during mitosis. The endosomal pathway is a highly dynamic intracellular transport system, which consists of vesicular compartments and tubular extensions, although it is currently unclear whether incoming viruses specifically alter the endocytic machinery. In this study, using MICAL-L1 as a marker for tubulating endosomes, we show that incoming HPV-16 virions induce a profound alteration in global levels of endocytic tubulation...
March 15, 2018: Journal of Virology
https://www.readbyqxmd.com/read/29229824/molecular-mechanism-for-the-subversion-of-the-retromer-coat-by-the-legionella-effector-ridl
#8
Miguel Romano-Moreno, Adriana L Rojas, Chad D Williamson, David C Gershlick, María Lucas, Michail N Isupov, Juan S Bonifacino, Matthias P Machner, Aitor Hierro
Microbial pathogens employ sophisticated virulence strategies to cause infections in humans. The intracellular pathogen Legionella pneumophila encodes RidL to hijack the host scaffold protein VPS29, a component of retromer and retriever complexes critical for endosomal cargo recycling. Here, we determined the crystal structure of L. pneumophila RidL in complex with the human VPS29-VPS35 retromer subcomplex. A hairpin loop protruding from RidL inserts into a conserved pocket on VPS29 that is also used by cellular ligands, such as Tre-2/Bub2/Cdc16 domain family member 5 (TBC1D5) and VPS9-ankyrin repeat protein for VPS29 binding...
December 26, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29210454/the-functional-roles-of-retromer-in-parkinson-s-disease
#9
REVIEW
Yi Cui, Zhe Yang, Rohan D Teasdale
The endosomal system is critical for the maintenance of intracellular homeostasis, and defects in this system are often linked to neurological disorders. The retromer complex is a critical coordinator of endosomal dynamics and has functional roles in multiple cellular processes through sorting cargoes from endosomes to the trans-Golgi network (TGN) or to the plasma membrane. Mammalian retromer comprises a core Vps26-Vps35-Vps29 trimer and associates with a range of proteins to generate endosomal tubular-vesicular carriers...
December 6, 2017: FEBS Letters
https://www.readbyqxmd.com/read/29146912/structural-insights-into-legionella-ridl-vps29-retromer-subunit-interaction-reveal-displacement-of-the-regulator-tbc1d5
#10
Kevin Bärlocher, Cedric A J Hutter, A Leoni Swart, Bernhard Steiner, Amanda Welin, Michael Hohl, François Letourneur, Markus A Seeger, Hubert Hilbi
Legionella pneumophila can cause Legionnaires' disease and replicates intracellularly in a distinct Legionella-containing vacuole (LCV). LCV formation is a complex process that involves a plethora of type IV-secreted effector proteins. The effector RidL binds the Vps29 retromer subunit, blocks retrograde vesicle trafficking, and promotes intracellular bacterial replication. Here, we reveal that the 29-kDa N-terminal domain of RidL (RidL2-281 ) adopts a "foot-like" fold comprising a protruding β-hairpin at its "heel"...
November 16, 2017: Nature Communications
https://www.readbyqxmd.com/read/29135085/retromer-and-the-cation-independent-mannose-6-phosphate-receptor-time-for-a-trial-separation
#11
Matthew N J Seaman
The retromer cargo-selective complex (CSC) comprising Vps35, Vps29 and Vps26 mediates the endosome-to-Golgi retrieval of the cation-independent mannose 6-phosphate receptor (CIMPR). Or does it? Recently published data have questioned the validity of this long-established theory. Here, the evidence for and against a role for the retromer CSC in CIMPR endosome-to-Golgi retrieval is examined in the light of the new data that the SNX-BAR dimer is actually responsible for CIMPR retrieval.
February 2018: Traffic
https://www.readbyqxmd.com/read/28935632/cargo-selective-snx-bar-proteins-mediate-retromer-trimer-independent-retrograde-transport
#12
Arunas Kvainickas, Ana Jimenez-Orgaz, Heike Nägele, Zehan Hu, Jörn Dengjel, Florian Steinberg
The retromer complex, which recycles the cation-independent mannose 6-phosphate receptor (CI-MPR) from endosomes to the trans-Golgi network (TGN), is thought to consist of a cargo-selective VPS26-VPS29-VPS35 trimer and a membrane-deforming subunit of sorting nexin (SNX)-Bin, Amphyphysin, and Rvs (BAR; SNX-BAR) proteins. In this study, we demonstrate that heterodimers of the SNX-BAR proteins, SNX1, SNX2, SNX5, and SNX6, are the cargo-selective elements that mediate the retrograde transport of CI-MPR from endosomes to the TGN independently of the core retromer trimer...
November 6, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28898487/structural-and-thermodynamic-characterization-of-metal-binding-in-vps29-from-entamoeba-histolytica-implication-in-retromer-function
#13
Vijay Kumar Srivastava, Rupali Yadav, Natsuki Watanabe, Priya Tomar, Madhumita Mukherjee, Samudrala Gourinath, Kumiko Nakada-Tsukui, Tomoyoshi Nozaki, Sunando Datta
Vps29 is the smallest subunit of retromer complex with metallo-phosphatase fold. Although the role of metal in Vps29 is in quest, its metal binding mutants has been reported to affect the localization of the retromer complex in human cells. In this study, we report the structural and thermodynamic consequences of these mutations in Vps29 from the protozoan parasite, Entamoeba histolytica (EhVps29). EhVps29 is a zinc binding protein as revealed by X-ray crystallography and isothermal titration calorimetry. The metal binding pocket of EhVps29 exhibits marked differences in its 3-dimensional architecture and metal coordination in comparison to its human homologs and other metallo-phosphatases...
November 2017: Molecular Microbiology
https://www.readbyqxmd.com/read/28892079/retriever-is-a-multiprotein-complex-for-retromer-independent-endosomal-cargo-recycling
#14
Kerrie E McNally, Rebecca Faulkner, Florian Steinberg, Matthew Gallon, Rajesh Ghai, David Pim, Paul Langton, Neil Pearson, Chris M Danson, Heike Nägele, Lindsey L Morris, Amika Singla, Brittany L Overlee, Kate J Heesom, Richard Sessions, Lawrence Banks, Brett M Collins, Imre Berger, Daniel D Billadeau, Ezra Burstein, Peter J Cullen
Following endocytosis into the endosomal network, integral membrane proteins undergo sorting for lysosomal degradation or are retrieved and recycled back to the cell surface. Here we describe the discovery of an ancient and conserved multiprotein complex that orchestrates cargo retrieval and recycling and, importantly, is biochemically and functionally distinct from the established retromer pathway. We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer...
October 2017: Nature Cell Biology
https://www.readbyqxmd.com/read/28757549/updated-insight-into-the-physiological-and-pathological-roles-of-the-retromer-complex
#15
REVIEW
Yakubu Saddeeq Abubakar, Wenhui Zheng, Stefan Olsson, Jie Zhou
Retromer complexes mediate protein trafficking from the endosomes to the trans-Golgi network (TGN) or through direct recycling to the plasma membrane. In yeast, they consist of a conserved trimer of the cargo selective complex (CSC), Vps26-Vps35-Vps29 and a dimer of sorting nexins (SNXs), Vps5-Vps17. In mammals, the CSC interacts with different kinds of SNX proteins in addition to the mammalian homologues of Vps5 and Vps17, which further diversifies retromer functions. The retromer complex plays important roles in many cellular processes including restriction of invading pathogens...
July 25, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28110103/the-retromer-complex-system-in-a-transgenic-mouse-model-of-ad-influence-of-age
#16
Jin Chu, Domenico Praticò
Deficiencies of the retrograde transport mediated by the retromer complex have been described in Alzheimer's disease (AD). Genetic manipulation of retromer modulates brain amyloidosis in Tg2576 mice. However, whether the complex is altered during the development of the AD-like phenotype remains unknown. In this study we assayed the expression levels of the vacuolar sorting protein 35 (VPS35), VPS26, VPS29, and its cargo proteins, cation independent mannose 6-phosphate receptor, sortilin-related receptor in brains of Tg2576 and controls at the ages of 3, 8, and 14 months...
April 2017: Neurobiology of Aging
https://www.readbyqxmd.com/read/27827364/structural-and-mechanistic-insights-into-regulation-of-the-retromer-coat-by-tbc1d5
#17
Da Jia, Jin-San Zhang, Fang Li, Jing Wang, Zhihui Deng, Mark A White, Douglas G Osborne, Christine Phillips-Krawczak, Timothy S Gomez, Haiying Li, Amika Singla, Ezra Burstein, Daniel D Billadeau, Michael K Rosen
Retromer is a membrane coat complex that is recruited to endosomes by the small GTPase Rab7 and sorting nexin 3. The timing of this interaction and consequent endosomal dynamics are thought to be regulated by the guanine nucleotide cycle of Rab7. Here we demonstrate that TBC1d5, a GTPase-activating protein (GAP) for Rab7, is a high-affinity ligand of the retromer cargo selective complex VPS26/VPS29/VPS35. The crystal structure of the TBC1d5 GAP domain bound to VPS29 and complementary biochemical and cellular data show that a loop from TBC1d5 binds to a conserved hydrophobic pocket on VPS29 opposite the VPS29-VPS35 interface...
November 9, 2016: Nature Communications
https://www.readbyqxmd.com/read/27528657/atypical-parkinsonism-associated-retromer-mutant-alters-endosomal-sorting-of-specific-cargo-proteins
#18
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
https://www.readbyqxmd.com/read/27103185/multiple-roles-of-varp-in-endosomal-trafficking-rabs-retromer-components-and-r-snare-vamp7-meet-on-varp
#19
REVIEW
Mitsunori Fukuda
VARP (VPS9-ankyrin-repeat protein, also known as ANKRD27) was originally identified as an N-terminal VPS9 (vacuolar protein sorting 9)-domain-containing protein that possesses guanine nucleotide exchange factor (GEF) activity toward small GTPase Rab21 and contains two ankyrin repeat (ANKR) domains in its central region. A number of VARP-interacting molecules have been identified during the past five years, and considerable attention is now being directed to the multiple roles of VARP in endosomal trafficking...
July 2016: Traffic
https://www.readbyqxmd.com/read/27064065/unconventional-endosome-like-compartment-and-retromer-complex-in-toxoplasma-gondii-govern-parasite-integrity-and-host-infection
#20
Lamba Omar Sangaré, Tchilabalo Dilezitoko Alayi, Benoit Westermann, Agnes Hovasse, Fabien Sindikubwabo, Isabelle Callebaut, Elisabeth Werkmeister, Frank Lafont, Christian Slomianny, Mohamed-Ali Hakimi, Alain Van Dorsselaer, Christine Schaeffer-Reiss, Stanislas Tomavo
Membrane trafficking pathways play critical roles in Apicomplexa, a phylum of protozoan parasites that cause life-threatening diseases worldwide. Here we report the first retromer-trafficking interactome in Toxoplasma gondii. This retromer complex includes a trimer Vps35-Vps26-Vps29 core complex that serves as a hub for the endosome-like compartment and parasite-specific proteins. Conditional ablation of TgVps35 reveals that the retromer complex is crucial for the biogenesis of secretory organelles and for maintaining parasite morphology...
April 11, 2016: Nature Communications
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