Journal
BIOCHEMISTRY
Volume 41, Issue 16, Pages 5067-5074Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi015940q
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Funding
- NCRR NIH HHS [RR11823] Funding Source: Medline
- NIGMS NIH HHS [R01 GM059167, R01 GM055316, GM59167, GM55316] Funding Source: Medline
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Covalent attachment of ubiquitin is well-known to target proteins for degradation. Here, mass spectrometry was used to identify the site of ubiquitination in Gpa1, the G protein alpha subunit in yeast Saccharomyces cerevisiae. The modified residue is located at Lys165 within the alpha-helical domain of Galpha, a region of unknown function. Substitution of Lys165 with Arg (Gpa1(K165R)) results in a substantial decrease in ubiquitination. In addition, yeast expressing the Gpa1(K165R) mutant are moderately resistant to pheromone in growth inhibition assays-a phenotype consistent with enhanced Galpha signaling activity. These findings indicate that the alpha-helical domain may serve to regulate the turnover of Gpa1.
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