Ravid T~Hochstrasser M, 2006

Pubmed ID 16437165
Title Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways.
Authors Tommer Ravid, Stefan G Kreft, Mark Hochstrasser
Abstract The yeast Doa10 ubiquitin (Ub) ligase resides in the endoplasmic reticulum (ER)/nuclear envelope (NE), where it functions in ER-associated degradation (ERAD). Doa10 substrates include non-ER proteins such as the transcription factor Mat alpha2. Here, we expand the range of Doa10 substrates to include a defective kinetochore component, a mutant NE membrane protein, and a substrate-regulated human ER enzyme. For all these substrates, Doa10 requires two Ub-conjugating enzymes, Ubc6 and Ubc7, as well as the Ubc7 cofactor Cue1. Based on a novel genomic screen of a comprehensive gene deletion library and other data, these four proteins appear to be the only nonessential and nonredundant factors generally required for Doa10-mediated ubiquitination. Notably, the Cdc48 ATPase facilitates degradation of membrane-embedded Doa10 substrates, but is not required for any tested soluble Doa10 substrates. This distinction is maintained even when comparing membrane and soluble proteins bearing the same degradation signal. Thus, while Doa10 ubiquitinates both membrane and soluble proteins, the mechanisms of subsequent proteasome targeting differ.
Citation EMBO J. 2006; 25:533-43


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Papers Phenotype Conditions Collection Tested mutants Data Details
Ravid T~Hochstrasser M, 2006 abundance of a specific protein/peptide (Deg1) standard [standard] hap a ~4,753 Discrete

Curation history

March 21, 2014 Tested strains to request.
March 21, 2014 Data waiting for tested.
March 31, 2014 Tested strains requested.
Nov. 11, 2014 Tested strains requested.
Jan. 28, 2015 Tested strains abandoned.
Jan. 28, 2015 Data to load.
Jan. 29, 2017 Data loaded.