Search results for "RAB3GAP"

showing 2 items of 2 documents

The integration of autophagy and cellular trafficking pathways via RAB GAPs.

2015

Macroautophagy is a conserved degradative pathway in which a double-membrane compartment sequesters cytoplasmic cargo and delivers the contents to lysosomes for degradation. Efficient formation and maturation of autophagic vesicles, so-called phagophores that are precursors to autophagosomes, and their subsequent trafficking to lysosomes relies on the activity of small RAB GTPases, which are essential factors of cellular vesicle transport systems. The activity of RAB GTPases is coordinated by upstream factors, which include guanine nucleotide exchange factors (RAB GEFs) and RAB GTPase activating proteins (RAB GAPs). A role in macroautophagy regulation for different TRE2-BUB2-CDC16 (TBC) dom…

0301 basic medicineautophagyRAB GTPaseGTPase-activating proteinGTPaseBiologyRAB GAP03 medical and health sciences0302 clinical medicineAnimalsGuanine Nucleotide Exchange FactorsHumansRAB3GAPMolecular Biologyautophagosome formationVesicleAutophagyCellular VesiclefungiGTPase-Activating ProteinsView and CommentaryCell BiologyTransport proteinCell biologyProtein Transport030104 developmental biologyrab GTP-Binding Proteinsvesicle traffickingGuanine nucleotide exchange factorRabLysosomes030217 neurology & neurosurgeryAutophagy
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RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy

2014

Macroautophagy is a degradative pathway that sequesters and transports cytosolic cargo in autophagosomes to lysosomes, and its deterioration affects intracellular proteostasis. Membrane dynamics accompanying autophagy are mostly elusive and depend on trafficking processes. RAB GTPase activating proteins (RABGAPs) are important factors for the coordination of cellular vesicle transport systems, and several TBC (TRE2-BUB2-CDC16) domain-containing RABGAPs are associated with autophagy. Employing C. elegans and human primary fibroblasts, we show that RAB3GAP1 and RAB3GAP2, which are components of the TBC domain-free RAB3GAP complex, influence protein aggregation and affect autophagy at basal an…

GTPase-activating proteinlipid dropletsrab3 GTP-Binding ProteinsATG16L1DMSO dimethyl sulfoxideFEZ20302 clinical medicineATG autophagy-relatedPhagosomesDAPI 4’ 6-diamidino-2-phenylindoleSQSTM1 sequestosome 1ATG16L1MAP1LC3 microtubule-associated protein 1 light chain 3GFP green fluorescent protein0303 health sciencesGABARAP GABA(A) receptor-associated proteinGTPase-Activating ProteinsCell biologyRAB3GAP1RAB3GAP2RABGAP RAB GTPase activating proteinATG3autophagyCALCOCO2 calcium binding and coiled-coil domain 2Basic Research PaperseV empty vectorATG8ATG5PBS phosphate-buffered salineBiologyPE phosphatidylethanolamineTBC domain TRE2-BUB2-CDC16 domainBAG3GEF guanine nucleotide exchange factor03 medical and health sciencesC. elegans Caenorhabditis elegansAnimalsHumansCaenorhabditis elegansMolecular Biology030304 developmental biologySirolimusDPH 1 6-diphenyl-1 3 5-hexatrieneproteostasisAutophagyBiological TransportCell BiologyFEZ1Bafi bafilomycin A1FEZ fasciculation and elongation protein zetaNBR1 neighbor of BRCA1 gene 1ProteostasissiRNA small interfering RNABSA bovine serum albuminRabLysosomes030217 neurology & neurosurgeryAutophagy
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