Regional Expression of Protein Phosphatase Type 1 and 2A Catalytic Subunit Isoforms in the Human Heart

2000 ◽  
Vol 32 (12) ◽  
pp. 2349-2359 ◽  
Author(s):  
Hartmut Lüss ◽  
Oliver Klein-Wiele ◽  
Peter Boknı́k ◽  
Stefan Herzig ◽  
Jörg Knapp ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Human Heart ◽  
Catalytic Subunit ◽  
Protein Phosphatase Type 1 ◽  
Subunit Isoforms ◽  
Protein Phosphatase Type

Enhanced expression of catalytic subunit isoform PP1γ1 of protein phosphatase type 1 associated with malignancy of osteogenic tumor

1995 ◽  
Vol 89 (1) ◽  
pp. 1-6
Author(s):  
Kenichi Sogawa ◽  
Takahisa Yamada ◽  
Shiro Oka ◽  
Kojiro Kawasaki ◽  
Satoshi Mori ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Protein Phosphatase Type 1 ◽  
Enhanced Expression ◽  
Protein Phosphatase Type

scholarly journals The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.

1993 ◽  
Vol 7 (4) ◽  
pp. 555-569 ◽  
Author(s):  
T Durfee ◽  
K Becherer ◽  
P L Chen ◽  
S H Yeh ◽  
Y Yang ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Retinoblastoma Protein ◽  
Catalytic Subunit ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Genetic Interactions Between REG1/HEX2 and GLC7, the Gene Encoding the Protein Phosphatase Type 1 Catalytic Subunit in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 119-127 ◽  
Author(s):  
Dongqing Huang ◽  
Kristin T Chun ◽  
Mark G Goebl ◽  
Peter J Roach
Keyword(s):  
Protein Phosphatase ◽  
Glucose Repression ◽  
Glycogen Synthesis ◽  
Catalytic Subunit ◽  
Loss Of Function ◽  
Gene Encoding ◽  
Glycogen Accumulation ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

Abstract Mutations in GLC7, the gene encoding the type 1 protein phosphatase catalytic subunit, cause a variety of abberrant phenotypes in yeast, such as impaired glycogen synthesis and relief of glucose repression of the expression of some genes. Loss of function of the REG1/HEX2 gene, necessary for glucose repression of several genes, was found to suppress the glycogendeficient phenotype of the glc7-1 allele. Deletion of REG1 in a wild-type background led to overaccumulation of glycogen as well as slow growth and an enlarged cell size. However, loss of REG1 did not suppress other phenotypes associated with GLC7 mutations, such as inability to sporulate or, in cells bearing the glc7Y-170 allele, lack of growth at 14°. The effect of REG1 deletion on glycogen accumulation is not simply due to derepression of glucose-repressed genes, although it does require the presence of SAF1, which encodes a protein kinase essential for expression of glucose-repressed genes and for glycogen accumulation. We propose that REG1 has a role in controlling glycogen accumulation.

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.

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