Results 51 to 60 of about 9,787 (196)

Hyperleucinemia causes hippocampal retromer deficiency linking diabetes to Alzheimer's disease

Neurobiology of Disease, 2014
Type 2 diabetes (T2D) is a major risk factor for late-onset Alzheimer's disease (AD). A variety of metabolic changes related to T2D (e.g. hyperinsulinemia, hyperglycemia, and elevated branched-chain amino acids) have been proposed as mechanistic links ...
Michael V. Morabito, Diego E. Berman, Remy T. Schneider, Yiying Zhang, Rudolph L. Leibel, Scott A. Small   +5 more
doaj   +1 more source

Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health

Nature Communications, 2023
Retromer controls cellular homeostasis through regulating integral membrane protein sorting and transport and by controlling maturation of the endo-lysosomal network.
James L. Daly, Chris M. Danson, Philip A. Lewis, Lu Zhao, Sara Riccardo, Lucio Di Filippo, Davide Cacchiarelli, Daehoon Lee, Stephen J. Cross, Kate J. Heesom, Wen-Cheng Xiong, Andrea Ballabio, James R. Edgar, Peter J. Cullen   +13 more
doaj   +1 more source

Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers [PDF]

, 2017
Missense mutations in leucine-rich repeat kinase 2 (LRRK2) are pathogenic for familial Parkinson's disease. However, it is unknown whether levels of LRRK2 protein in the brain are altered in patients with LRRK2-associated Parkinson's disease.
Dzamko, N, Halliday, GM, Hasegawa, K, Holton, JL, Jeremy Nichols, R, Mash, DC, Murayama, S, Paul, J, Perera, G, Takahashi-Fujigasaki, J, Uchino, A, Vonsattel, G, Zhao, Y   +12 more
core   +1 more source

Toxoplasma Retromer Is Here to Stay [PDF]

Trends in Parasitology, 2016
How the protozoan pathogen Toxoplasma gondii and related parasites shuttle proteins through their intricate system of endomembranous compartments remains unclear. Sangaré et al. show that the Toxoplasma retromer complex is essential for parasite viability through its role in protein targeting to multiple locales and its interactions with newly ...
Olivia L, McGovern, Vern B, Carruthers
openaire   +2 more sources

Resolving the homology-function relationship through comparative genomics of membrane-trafficking machinery and parasite cell biology [PDF]

, 2016
With advances in DNA sequencing technology, it is increasingly common and tractable to informatically look for genes of interest in the genomic databases of parasitic organisms and infer cellular states.
Aaron P. Turkewitz, Agop-Nersesian, Agop-Nersesian, Asaoka, Asaoka, Barlowe, Barth, Bashline, Baum, Bañuelos, Beck, Bennett, Biller, Blanc, Bonifacino, Bonifacino, Bradley, Braun, Bright, Briguglio, Briguglio, Buczynski, Cai, Cai, Cardona-López, Castillo-Romero, Charette, Chavrier, Chen, Chen, Choi, Chow, Christen M. Klinger, Chung, Cui, Dacks, Dacks, Dettmer, Di Rubbo, Dieckmann, Diekmann, Dutta, Ebine, Ebine, Elde, Elias, Elias, Elliott, Emily K. Herman, Essid, Ezougou, Fan, Faso, Feraru, Field, Field, Field, Fitch, Francia, Fuji, Gabernet-Castello, Gadeyne, Gao, Gao, Giansanti, Gillingham, Gotthardt, Gotthardt, Haas, Hall, Harding, Harper, Harris, Hashiguchi, Henne, Herman, Hirst, Hirst, Hirst, Huotari, Il Kwon, Il Kwon, Inmaculada Ramirez-Macias, Isono, Jackson, Jacobs, Jaillais, Jimenez-Ruiz, Joel B. Dacks, Kang, Katsiarimpa, Kibria, Kim, Kleine-Vehn, Klinger, Knödler, Kolb, Komsic-Buchmann, Komsic-Buchmann, Koonin, Koumandou, Koumandou, Krai, Kremer, Kumar, Lee, Lefkir, Lefkir, Leung, Lunn, López-Reyes, Macro, Manil-Segalén, Manna, Manna, Marion, Mark C. Field, Mattei, McGugan, Mercanti, Miranda, Miras, Mitra, Morrison, Munch, Müller-Taubenberger, Nakada-Tsukui, Neuhaus, Ngô, Ngô, Niemes, Nishimura, Niyogi, Nodzynski, Nordmann, Okada, Okada, Oliviusson, Ouologuem, Pal, Pal, Park, Parkinson, Parussini, Perez-Linero, Pourcher, Preuss, Preuss, Price, Ralston, Rauch, Reider, Reyes, Rink, Rivero, Rivero, Robibaro, Robinson, Robinson, Rojas, Rupper, Rupper, Saito-Nakano, Sangaré, Scheuring, Schlacht, Schlacht, Seaman, Seaman, Shahriari, Shimada, Silverman, Silverman, Singh, Sloves, Sohn, Song, Sosa, Spitzer, Spitzer, Spitzer, Srinivasan, Stenmark, Szumlanski, Tarnita, Tazeh, Teh, Teixeira, Temesvari, Thole, Tomavo, Touz, Touz, Ueda, Ueda, Ulrich, Viotti, Wampfler, Wang, Wang, Welz, Wen, Winter, Woo, Wurmser, Yamaoka, Yamazaki, Yang, Zelazny, Zelazny, Zoltner   +210 more
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EHDs meet the retromer [PDF]

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, Naslavsky, Naava, Caplan, Steve   +2 more
openaire   +2 more sources

Retromer regulates HIV-1 envelope glycoprotein trafficking and incorporation into virions.

PLoS Pathogens, 2014
The envelope glycoprotein (Env) of the Human Immunodeficiency Virus Type-1 (HIV-1) is a critical determinant of viral infectivity, tropism and is the main target for humoral immunity; however, little is known about the cellular machinery that directs Env
Elisabetta Groppelli, Alice C Len, Luke A Granger, Clare Jolly   +3 more
doaj   +1 more source

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, Evelyne Ruchti, Wei Jiao, Greta Limoni, Catherine MacLachlan, Scott A. Small, Graham Knott, Ismael Santa-Maria, Brian D. McCabe   +8 more
doaj   +1 more source

Atypical parkinsonism-associated retromer mutant alters endosomal sorting of specific cargo proteins [PDF]

, 2016
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.
Adam P. Jellett, Arighi, Balana, Bean, Bean, Brett M. Collins, Burd, Cai, Chan, Chapin, Chris M. Danson, Cullen, Damseh, Frances C. Tilley, Freeman, Gallon, Gomez, Gustavsson, Harbour, Harbour, Hesketh, Ian McGough, Joubert, Kate J. Heesom, Kerr, Kevin A. Wilkinson, Kirsty J. McMillan, Lauffer, MacLeod, Matthew Gallon, McGough, McGough, Muhammad, Peter J. Cullen, Phillips-Krawczak, Popoff, Rovelet-Lecrux, Seaman, Seaman, Seaman, Seaman, Shannon, Shi, Small, Steinberg, Steinberg, Temkin, Thomas Clairfeuille, Vardarajan, Vilariño-Güell, Vilariño-Güell, Wang, Yoshimura, Zavodszky, Zimprich   +54 more
core   +3 more sources

Retromer Dysfunction and Neurodegenerative Disease [PDF]

Current Genomics, 2018
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).
openaire   +2 more sources