scholarly journals The Pyridinyl Imidazole Inhibitor SB203580 Blocks Phosphoinositide-dependent Protein Kinase Activity, Protein Kinase B Phosphorylation, and Retinoblastoma Hyperphosphorylation in Interleukin-2-stimulated T Cells Independently of p38 Mitogen-activated Protein Kinase

2000 ◽  
Vol 275 (10) ◽  
pp. 7395-7402 ◽  
Author(s):  
Ferdinand V. Lali ◽  
Abigail E. Hunt ◽  
Sarah J. Turner ◽  
Brian M. J. Foxwell
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase B ◽  
Interleukin 2 ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Mitogen Activated Protein ◽  
Dependent Protein ◽  
Pyridinyl Imidazole

scholarly journals Activation of a Nuclear Cdc2-Related Kinase within a Mitogen-Activated Protein Kinase-Like TDY Motif by Autophosphorylation and Cyclin-Dependent Protein Kinase-Activating Kinase

2005 ◽  
Vol 25 (14) ◽  
pp. 6047-6064 ◽  
Author(s):  
Zheng Fu ◽  
Melanie J. Schroeder ◽  
Jeffrey Shabanowitz ◽  
Philipp Kaldis ◽  
Kasumi Togawa ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Localization ◽  
Kinase Activity ◽  
Catalytic Domain ◽  
Mitogen Activated Protein Kinase ◽  
Intestinal Cell ◽  
Dependent Protein Kinase ◽  
Mitogen Activated Protein ◽  
Dependent Protein

ABSTRACT Male germ cell-associated kinase (MAK) and intestinal cell kinase (ICK) are nuclear Cdc2-related kinases with nearly identical N-terminal catalytic domains and more divergent C-terminal noncatalytic domains. The catalytic domain is also related to mitogen-activated protein kinases (MAPKs) and contains a corresponding TDY motif. Nuclear localization of ICK requires subdomain XI and interactions of the conserved Arg-272, but not kinase activity or, surprisingly, any of the noncatalytic domain. Further, nuclear localization of ICK is required for its activation. ICK is activated by dual phosphorylation of the TDY motif. Phosphorylation of Tyr-159 in the TDY motif requires ICK autokinase activity but confers only basal kinase activity. Full activation requires additional phosphorylation of Thr-157 in the TDY motif. Coexpression of ICK with constitutively active MEK1 or MEK5 fails to increase ICK phosphorylation or activity, suggesting that MEKs are not involved. ICK and MAK are related to Ime2p in budding yeast, and cyclin-dependent protein kinase-activating kinase Cak1p has been placed genetically upstream of Ime2p. Recombinant Cak1p phosphorylates Thr-157 in the TDY motif of recombinant ICK and activates its activity in vitro. Coexpression of ICK with wild-type CAK1 but not kinase-inactive CAK1 in cells also increases ICK phosphorylation and activity. Our studies establish ICK as the prototype for a new group of MAPK-like kinases requiring dual phosphorylation at TDY motifs.

Tenellones A and B from aDiaporthesp.:  Two Highly Substituted Benzophenone Inhibitors of Parasite cGMP-Dependent Protein Kinase Activity

2005 ◽  
Vol 68 (4) ◽  
pp. 611-613 ◽  
Author(s):  
Chaowei Zhang ◽  
John G. Ondeyka ◽  
Kithsiri B. Herath ◽  
Ziqiang Guan ◽  
Javier Collado ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Dependent Protein

Analytical subcellular distribution of cAMP-dependent protein kinase activity in bull sperm

1984 ◽  
Vol 10 (4) ◽  
pp. 433-444 ◽  
Author(s):  
Claude C. Pariset ◽  
Jacqueline S. Weinman ◽  
Francoise T. Escaig ◽  
Michele Y. Guyot ◽  
Francine C. Iftode ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Subcellular Distribution ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Bull Sperm
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