| Title: | Degradation of G alpha by the N-end rule pathway |
| Address: | "Division of Biology, California Institute of Technology, Pasadena 91125" |
| ISSN/ISBN: | 0036-8075 (Print) 0036-8075 (Linking) |
| Abstract: | "The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Overexpression of targeting components of the N-end rule pathway in Saccharomyces cerevisiae inhibited the growth of haploid but not diploid cells. This ploidy-dependent toxicity was shown to result from enhanced degradation of Gpa1, the alpha subunit (G alpha) of a heterotrimeric guanine nucleotide-binding protein (G protein) that regulates cell differentiation in response to mating pheromones. Sst2, a protein whose absence renders cells hypersensitive to pheromone, was essential for degradation of G alpha but not other N-end rule substrates, suggesting the involvement of an indirect, or trans-, targeting mechanism. G alpha degradation by the N-end rule pathway adds another regulatory dimension to the multitude of signaling functions mediated by G proteins" |
| Keywords: | Cell Division Dipeptides/pharmacology Fungal Proteins/*metabolism GTP-Binding Proteins/*metabolism Guanosine Triphosphate/metabolism Half-Life Haploidy Ligases/*metabolism Saccharomyces cerevisiae/genetics/growth & development/*metabolism *Saccharomyces c; |
| Notes: | "MedlineMadura, K Varshavsky, A eng Research Support, U.S. Gov't, P.H.S. 1994/09/02 Science. 1994 Sep 2; 265(5177):1454-8. doi: 10.1126/science.8073290" |
