Peters LZ~Ben-Aroya S, 2013

Pubmed ID 23690178
Title Formation and dissociation of proteasome storage granules are regulated by cytosolic pH.
Authors Lee Zeev Peters, Rotem Hazan, Michal Breker, Maya Schuldiner, Shay Ben-Aroya
Abstract The 26S proteasome is the major protein degradation machinery of the cell and is regulated at many levels. One mode of regulation involves accumulation of proteasomes in proteasome storage granules (PSGs) upon glucose depletion. Using a systematic robotic screening approach in yeast, we identify trans-acting proteins that regulate the accumulation of proteasomes in PSGs. Our dataset was enriched for subunits of the vacuolar adenosine triphosphatase (V-ATPase) complex, a proton pump required for vacuole acidification. We show that the impaired ability of V-ATPase mutants to properly govern intracellular pH affects the kinetics of PSG formation. We further show that formation of other protein aggregates upon carbon depletion also is triggered in mutants with impaired activity of the plasma membrane proton pump and the V-ATPase complex. We thus identify cytosolic pH as a specific cellular signal involved both in the glucose sensing that mediates PSG formation and in a more general mechanism for signaling carbon source exhaustion.
Citation J. Cell Biol. 2013; 201:663-71


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Paper Phenotype Condition Medium Collection Tested mutants Data Details
Peters LZ~Ben-Aroya S, 2013 transport to/from protein storage granules (PSGs) (Rpn5-GFP) standard SD + Leu + Met hap a ~5,000 Discrete

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