Protein phosphatase type-1 regulatory subunits Reg1p and Reg2p act as signal transducers in the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae

2000 ◽  
Vol 263 (3) ◽  
pp. 411-422 ◽  
Author(s):  
H. Jiang ◽  
K. Tatchell ◽  
S. Liu ◽  
C. A. Michels
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Regulatory Subunits ◽  
Maltose Permease ◽  
Signal Transducers ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Protein Phosphatase Type 1 Regulates Ion Homeostasis in Saccharomyces cerevisiae

Genetics ◽  
2002 ◽  
Vol 160 (4) ◽  
pp. 1423-1437 ◽  
Author(s):  
Tara Williams-Hart ◽  
Xiaolin Wu ◽  
Kelly Tatchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Protein Phosphatase ◽  
Essential Gene ◽  
Ion Homeostasis ◽  
Iodide Uptake ◽  
Recessive Mutations ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

Abstract Protein phosphatase type 1 (PP1) is encoded by the essential gene GLC7 in Saccharomyces cerevisiae. glc7-109 (K259A, R260A) has a dominant, hyperglycogen defect and a recessive, ion and drug sensitivity. Surprisingly, the hyperglycogen phenotype is partially retained in null mutants of GAC1, GIP2, and PIG1, which encode potential glycogen-targeting subunits of Glc7. The R260A substitution in GLC7 is responsible for the dominant and recessive traits of glc7-109. Another mutation at this residue, glc7-R260P, confers only salt sensitivity, indicating that the glycogen and salt traits of glc7-109 are due to defects in distinct physiological pathways. The glc7-109 mutant is sensitive to cations, aminoglycosides, and alkaline pH and exhibits increased rates of l-leucine and 3,3′-dihexyloxacarbocyanine iodide uptake, but it is resistant to molar concentrations of sorbitol or KCl, indicating that it has normal osmoregulation. KCl suppresses the ion and drug sensitivities of the glc7-109 mutant. The CsCl sensitivity of this mutant is suppressed by recessive mutations in PMA1, which encodes the essential plasma membrane H+ATPase. Together, these results indicate that Glc7 regulates ion homeostasis by controlling ion transport and/or plasma membrane potential, a new role for Glc7 in budding yeast.

scholarly journals GAC1 may encode a regulatory subunit for protein phosphatase type 1 in Saccharomyces cerevisiae.

1992 ◽  
Vol 11 (1) ◽  
pp. 87-96 ◽  
Author(s):  
J.M. François ◽  
S. Thompson-Jaeger ◽  
J. Skroch ◽  
U. Zellenka ◽  
W. Spevak ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Regulatory Subunit ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Alanine-Scanning Mutagenesis of Protein Phosphatase Type 1 in the Yeast Saccharomyces cerevisiae

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 615-626 ◽  
Author(s):  
Stefanie H Baker ◽  
Debra L Frederick ◽  
Andrew Bloecher ◽  
Kelly Tatchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Protein Phosphatase ◽  
Diverse Range ◽  
Cycle Arrest ◽  
Protein Phosphatase Type 1 ◽  
Wide Range ◽  
Protein Phosphatase Type

Protein phosphatase type 1, encoded by GLC7 in Saccharomyces cerevisiae, is an essential serine/threonine phosphatase implicated in the regulation of a diverse array of physiological functions. We constructed and examined 20 mutant alleles of GLC7 in which codons encoding clusters of charged residues were changed to alanine codons. Three of 20 mutant alleles alter residues in the active site of the phosphatase and are unable to rescue the lethality of a glc7::LEU2 disruption. The 17 alleles that support growth confer a range of mutant traits including cell cycle arrest, 2-deoxyglucose resistance, altered levels of glycogen, sensitivity to high salt, and sporulation defects. For some traits, such as 2-deoxyglucose resistance and cell cycle arrest, the mutated residues map to specific regions of the protein whereas the mutated residues in glycogen-deficient mutants and sporulation-defective mutants are more widely distributed over the protein surface. Many mutants have complex phenotypes, each displaying a diverse range of defects. The wide range of phenotypes identified from the collection of mutant alleles is consistent with the hypothesis that Glc7p-binding proteins, which are thought to regulate the specificity of Glc7p, have overlapping binding sites on the surface of Glc7p. This could account for the high level of sequence conservation found among type 1 protein phosphatases from different species.

scholarly journals Ectopic Expression of Inhibitors of Protein Phosphatase Type 1 (PP1) Can Be Used to Analyze Roles of PP1 in Drosophila Development

Genetics ◽  
2003 ◽  
Vol 164 (1) ◽  
pp. 235-245
Author(s):  
Daimark Bennett ◽  
Balázs Szöőr ◽  
Sascha Gross ◽  
Natalia Vereshchagina ◽  
Luke Alphey
Keyword(s):  
Protein Phosphatase ◽  
Muscle Development ◽  
Ectopic Expression ◽  
High Specificity ◽  
Type I ◽  
Protein Phosphatase Type 1 ◽  
Mitotic Figures ◽  
Protein Phosphatase Type

Abstract We have identified two proteins that bind with high specificity to type 1 serine/threonine protein phosphatase (PP1) and have exploited their inhibitory properties to develop an efficient and flexible strategy for conditional inactivation of PP1 in vivo. We show that modest overexpression of Drosophila homologs of I-2 and NIPP1 (I-2Dm and NIPP1Dm) reduces the level of PP1 activity and phenotypically resembles known PP1 mutants. These phenotypes, which include lethality, abnormal mitotic figures, and defects in muscle development, are suppressed by coexpression of PP1, indicating that the effect is due specifically to loss of PP1 activity. Reactivation of I-2Dm:PP1c complexes suggests that inhibition of PP1 activity in vivo does not result in a compensating increase in synthesis of active PP1. PP1 mutants enhance the wing overgrowth phenotype caused by ectopic expression of the type II TGFβ superfamily signaling receptor Punt. Using I-2Dm, which has a less severe effect than NIPP1Dm, we show that lowering the level of PP1 activity specifically in cells overexpressing Punt is sufficient for wing overgrowth and that the interaction between PP1 and Punt requires the type I receptor Thick-veins (Tkv) but is not strongly sensitive to the level of the ligand, Decapentaplegic (Dpp), nor to that of the other type I receptors. This is consistent with a role for PP1 in antagonizing Punt by preventing phosphorylation of Tkv. These studies demonstrate that inhibitors of PP1 can be used in a tissue- and developmental-specific manner to examine the developmental roles of PP1.

Differential expression of protein phosphatase type 1 isotypes and nucleolin during cell cycle arrest

2007 ◽  
Vol 25 (4) ◽  
pp. 369-375 ◽  
Author(s):  
Hiroyuki Morimoto ◽  
Akiko Ozaki ◽  
Hirohiko Okamura ◽  
Kaya Yoshida ◽  
Bruna Rabelo Amorim ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Differential Expression ◽  
Protein Phosphatase ◽  
Cycle Arrest ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

Phosphorylation of the Protein Phosphatase Type 1 Inhibitor Protein CPI-17 by Protein Kinase C

2007 ◽  
pp. 209-224 ◽  
Author(s):  
Michael P. Walsh ◽  
Marija Susnjar ◽  
Jingti Deng ◽  
Cindy Sutherland ◽  
Eniko Kiss ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Inhibitor Protein ◽  
Kinase C ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type
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