scholarly journals Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

2015 ◽  
Vol 472 (3) ◽  
pp. 329-338 ◽  
Author(s):  
Malik M. Keshwani ◽  
Kendra L. Hailey ◽  
Brandon E. Aubol ◽  
Laurent Fattet ◽  
Maria L. McGlone ◽  
...  
Keyword(s):  
Cell Division ◽  
Protein Kinase ◽  
Nuclear Protein ◽  
Cell Division Cycle ◽  
Protein Substrates ◽  
Docking Mechanism ◽  
Physiological Substrates

CLK1 (Cdc (cell division cycle)2-like kinase 1) uses an oligomerization mechanism to recognize its physiological protein substrates.

Phosphorylation of Cdc28 and regulation of cell size by the protein kinase CKII in Saccharomyces cerevisiae

2000 ◽  
Vol 351 (1) ◽  
pp. 143-150 ◽  
Author(s):  
Gian Luigi RUSSO ◽  
Christian VAN DEN BOS ◽  
Ann SUTTON ◽  
Paola COCCETTI ◽  
Maurizio D. BARONI ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Division ◽  
Protein Kinase ◽  
Cell Size ◽  
Peptide Mapping ◽  
Budding Yeast ◽  
Cell Division Cycle ◽  
Yeast Saccharomyces Cerevisiae ◽  
Protein Kinase Ckii

The CDK (cyclin-dependent kinase) family of enzymes is required for the G1-to-S-phase and G2-to-M-phase transitions during the cell-division cycle of eukaryotes. We have shown previously that the protein kinase CKII catalyses the phosphorylation of Ser-39 in Cdc2 during the G1 phase of the HeLa cell-division cycle [Russo, Vandenberg, Yu, Bae, Franza and Marshak (1992) J. Biol. Chem. 267, 20317–20325]. To identify a functional role for this phosphorylation, we have studied the homologous enzymes in the budding yeast Saccharomyces cerevisiae. The S. cerevisiae homologue of Cdc2, Cdc28, contains a consensus CKII site (Ser-46), which is homologous with that of human Cdc2. Using in vitro kinase assays, metabolic labelling, peptide mapping and phosphoamino acid analysis, we demonstrate that this site is phosphorylated in Cdc28 in vivo as well in vitro. In addition, S. cerevisiae cells in which Ser-46 has been mutated to alanine show a decrease in both cell volume and protein content of 33%, and this effect is most pronounced in the stationary phase. Because cell size in S. cerevisiae is regulated primarily at the G1 stage, we suggest that CKII contributes to the regulation of the cell cycle in budding yeast by phosphorylation of Cdc28 as a checkpoint for G1 progression.

scholarly journals A pathway in the yeast cell division cycle linking protein kinase C (Pkc1) to activation of Cdc28 at START.

1996 ◽  
Vol 15 (12) ◽  
pp. 3040-3052 ◽  
Author(s):  
N. J. Marini ◽  
E. Meldrum ◽  
B. Buehrer ◽  
A. V. Hubberstey ◽  
D. E. Stone ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Cell Division ◽  
Protein Kinase ◽  
Yeast Cell ◽  
Cell Division Cycle ◽  
Kinase C

scholarly journals Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions

1985 ◽  
Vol 232 (3) ◽  
pp. 767-771 ◽  
Author(s):  
K Ahmed ◽  
S A Goueli ◽  
H G Williams-Ashman
Keyword(s):  
Catalytic Activity ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Nuclear Protein ◽  
Direct Stimulation ◽  
Protein Substrate ◽  
Protein Substrates ◽  
Effects Of Temperature ◽  
Independent Protein ◽  
Stimulation Of

The extent of direct stimulation by spermine of reactions catalysed by nuclear N1 and N2 protein kinases purified from liver and prostate depends critically on the nature of the protein substrate. The chemically inert Co(NH3)36+ ion exerts effects on protein kinase reactions similar to those of spermidine or spermine. This enhancement of the phosphorylation of various protein substrates by polyamines or Co(NH3)63+ by purified nuclear protein kinase preparations was studied in relation to effects of temperature, pH and other factors. The results provide further support for our hypothesis [Ahmed, Wilson, Goueli & Williams-Ashman (1978) Biochem. J. 176, 739-750] that the enhancement of certain protein kinase reactions by polycations relates primarily to their interaction with the protein substrate, yielding more favourable conformations for phosphorylation by the protein kinase, rather than a direct effect on its catalytic activity.

scholarly journals Zipper-interacting protein kinase interacts with human cell division cycle 14A phosphatase

2014 ◽  
Vol 11 (4) ◽  
pp. 2775-2780 ◽  
Author(s):  
WEI WU ◽  
HAIYING HU ◽  
ZI YE ◽  
MANCHEONG LEONG ◽  
MIN HE ◽  
...  
Keyword(s):  
Cell Division ◽  
Protein Kinase ◽  
Human Cell ◽  
Cell Division Cycle ◽  
Interacting Protein ◽  
Zipper Interacting Protein Kinase

Targeting nuclear protein TDP-43 by cell division cycle kinase 7 inhibitors: A new therapeutic approach for amyotrophic lateral sclerosis

2021 ◽  
Vol 210 ◽  
pp. 112968
Author(s):  
Elisa Rojas-Prats ◽  
Loreto Martinez-Gonzalez ◽  
Claudia Gonzalo-Consuegra ◽  
Nicole F. Liachko ◽  
Concepción Perez ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Cell Division ◽  
Therapeutic Approach ◽  
Nuclear Protein ◽  
Cell Division Cycle ◽  
Lateral Sclerosis

scholarly journals Protein kinase D1 induces G1‐phase cell‐cycle arrest independent of Checkpoint kinases by phosphorylating Cell Division Cycle Phosphatase 25

The Prostate ◽  
2019 ◽  
Vol 79 (9) ◽  
pp. 1053-1058
Author(s):  
Bita Nickkholgh ◽  
Sivanandane Sittadjody ◽  
Karina Ordonez ◽  
Michael Bryan Rothberg ◽  
K. C. Balaji
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Protein Kinase ◽  
Cell Cycle Arrest ◽  
Cell Division Cycle ◽  
Phase Cell ◽  
G1 Phase ◽  
Protein Kinase D1 ◽  
Checkpoint Kinases ◽  
Cycle Arrest
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