Dobzinski N~Gerst JE, 2015

Pubmed ID 26344761
Title Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways.
Authors Niv Dobzinski, Silvia G Chuartzman, Rachel Kama, Maya Schuldiner, Jeffrey E Gerst
Abstract Upon amino acid (AA) starvation and TOR inactivation, plasma-membrane-localized permeases rapidly undergo ubiquitination and internalization via the vacuolar protein sorting/multivesicular body (VPS-MVB) pathway and are degraded in the yeast vacuole. We now show that specific Golgi proteins are also directed to the vacuole under these conditions as part of a Golgi quality-control (GQC) process. The degradation of GQC substrates is dependent upon ubiquitination by the defective-for-SREBP-cleavage (DSC) complex, which was identified via genetic screening and includes the Tul1 E3 ligase. Using a model GQC substrate, GFP-tagged Yif1, we show that vacuolar targeting necessitates upregulation of the VPS pathway via proteasome-mediated degradation of the initial endosomal sorting complex required for transport, ESCRT-0, but not downstream ESCRT components. Thus, early cellular responses to starvation include the targeting of specific Golgi proteins for degradation, a phenomenon reminiscent of the inactivation of BTN1, the yeast Batten disease gene ortholog.
Citation Cell Rep 2015; 12:1876-86

Datasets

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Paper Phenotype Condition Reference Collection Tested mutants Data Details
Dobzinski N~Gerst JE, 2015 transport to vacuoles (GFP-Yif1) minimal complete -Ura [standard], temperature [26ºC] hap a 4,885 Discrete
Dobzinski N~Gerst JE, 2015 transport to vacuoles (GFP-Yif1) sirolimus [200 ug/L], minimal complete -Ura [standard], temperature [26ºC] hap a 4,885 Discrete

Curation history

Data

Feb. 12, 2018 Waiting for tested.
Feb. 26, 2018 Ready to load.
March 8, 2018 Loaded.

Tested strains

Feb. 12, 2018 To request.
Feb. 22, 2018 Request sent.
Feb. 26, 2018 Ready to load.
March 8, 2018 Loaded.