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Genetics, Vol. 172, 1427-1439, March 2006, Copyright © 2006
doi:10.1534/genetics.105.051698
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* Biology Department, Queens College and the Graduate School of CUNY, Flushing, New York 11367 and
Department of Biochemistry and Molecular Biology, LSU Health Sciences Center, Shreveport, Louisiana 71130
1 Corresponding author: Biology Department, Queens College of CUNY, 65-30 Kissena Blvd., Flushing, NY 11367.
E-mail: corinne_michels{at}qc.edu
yck2-2ts (yckts) strain with conditional Yck activity. Moreover, we provide evidence that Glc7Reg1 phosphatase acts as an upstream activator of Yck1,2 kinases in a novel signaling pathway that modulates kinase activity in response to carbon source availability. The yckts strain exhibits significantly reduced maltose transport activity despite apparently normal levels and cell surface localization of maltose permease protein. Glucose-induced internalization and rapid loss of maltose transport activity of Mal61/HAp-GFP are not observed in the yckts strain and maltose permease proteolysis is blocked. We show that a reg1
mutant exhibits a phenotype remarkably similar to that conferred by yckts. The reg1
phenotype is not enhanced in the yckts reg1
double mutant and is suppressed by increased Yck1,2p dosage. Further, although Yck2p localization and abundance do not change in the reg1
mutant, Yck1,2 kinase activity, as assayed by glucose-induced HXT1 expression and Mth1 repressor stability, is substantially reduced in the reg1
strain. This article has been cited by other articles:
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E. M. Rubenstein and M. C. Schmidt Mechanisms Regulating the Protein Kinases of Saccharomyces cerevisiae Eukaryot. Cell, April 1, 2007; 6(4): 571 - 583. [Full Text] [PDF] |
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