SCH9, a putative protein kinase from Saccharomyces cerevisiae, affects HOT1 -stimulated recombination

2004 ◽  
Vol 272 (3) ◽  
pp. 264-274 ◽  
Author(s):  
R. Prusty ◽  
R. L. Keil
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Putative Protein ◽  
Putative Protein Kinase

Suppression of Temperature-Sensitive RAS in S.cerevisiae by a Putative Protein Kinase

ras Oncogenes ◽  
1989 ◽  
pp. 93-97 ◽  
Author(s):  
Elena Carra ◽  
Pietro Masturzo ◽  
Alessandra Vitelli ◽  
Emanuele Burderi ◽  
Irene Lambrinoudaki ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Temperature Sensitive ◽  
Putative Protein ◽  
Putative Protein Kinase

scholarly journals The Acidic Region and Conserved Putative Protein Kinase C Phosphorylation Site in Nef Are Important for SIV Replication in Rhesus Macaques

Virology ◽  
1999 ◽  
Vol 257 (1) ◽  
pp. 138-155 ◽  
Author(s):  
Silke Carl ◽  
A.John Iafrate ◽  
Sabine M. Lang ◽  
Christiane Stahl-Hennig ◽  
Eva M. Kuhn ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rhesus Macaques ◽  
Phosphorylation Site ◽  
Putative Protein ◽  
Kinase C ◽  
Acidic Region ◽  
Putative Protein Kinase

Identifying tumor suppressors in genetic mosaics: the Drosophila lats gene encodes a putative protein kinase

Development ◽  
1995 ◽  
Vol 121 (4) ◽  
pp. 1053-1063 ◽  
Author(s):  
T. Xu ◽  
W. Wang ◽  
S. Zhang ◽  
R.A. Stewart ◽  
W. Yu
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Tumor Suppressors ◽  
Sequence Similarity ◽  
Developmental Defects ◽  
Genetic Mosaics ◽  
Putative Protein ◽  
Powerful Approach ◽  
Mutant Cells ◽  
Putative Protein Kinase

We have identified recessive overproliferation mutations by screening and examining clones of mutant cells in genetic mosaics of the fruitfly Drosophila melanogaster. This type of screen provides a powerful approach for identifying and studying potential tumor suppressors. One of the identified genes, lats, has been cloned and encodes a putative protein kinase that shares high levels of sequence similarity with three proteins in budding yeast and Neurospora that are involved in regulation of the cell cycle and growth. Mutations in lats cause dramatic overproliferation phenotypes and various developmental defects in both mosaic animals and homozygous mutants.

Differential effects of putative protein kinase C inhibitors on contraction of rat aortic smooth muscle

1993 ◽  
Vol 264 (4) ◽  
pp. H1300-H1306 ◽  
Author(s):  
Y. Shimamoto ◽  
H. Shimamoto ◽  
C. Y. Kwan ◽  
E. E. Daniel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Induced Response ◽  
Dependent Manner ◽  
Contractile Responses ◽  
Putative Protein ◽  
Calphostin C ◽  
Kinase C ◽  
Putative Protein Kinase

We investigated effects of three kinds of putative protein kinase C (PKC) inhibitors, calphostin C, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7), and stauro-sporine, on aortic muscle contractions induced by KCl, phenylephrine, 12-O-tetradecanoylphorbol-13-acetate (TPA), and phorbol 12, 13-dibutyrate (PDBu). Calphostin C noncompetitively inhibited TPA-induced contractions in a concentration-dependent manner. At 10(-6) M, calphostin C completely abolished responses to TPA and also effectively inhibited PDBu-induced contractions. Such a concentration of calphostin C had no effect on KCl-induced contractions but decreased the maximal tension of phenylephrine-induced response curve by 35.3 +/- 6.6% H-7 (10(-5) M had little effect on TPA-induced contraction but significantly inhibited contractile responses to phenylephrine and KCl. Staurosporine (10(-8) M, 3 x 10(-8) M) inhibited contractile responses to KCl, phenylephrine, and TPA. We suggest that staurosporine and H-7, which are known to act on the catalytic domain of PKC carrying high degree of sequence homology with other protein kinases, are relatively nonselective for PKC. On the other hand, calphostin C acting on the regulatory domain of PKC, which is distinct from other protein kinases, may serve as a relatively more selective PKC inhibitor.

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