scholarly journals Cell Division Cycle 7-Related Protein Kinase

2020 ◽  
Author(s):  
Keyword(s):  
Cell Division ◽  
Protein Kinase ◽  
Cell Division Cycle ◽  
Related Protein ◽  
Cell Division Cycle 7

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.

Cell Division Cycle 7 Kinase Inhibitors: 1H-Pyrrolo[2,3-b]pyridines, Synthesis and Structure−Activity Relationships

2009 ◽  
Vol 52 (14) ◽  
pp. 4380-4390 ◽  
Author(s):  
Antonella Ermoli ◽  
Alberto Bargiotti ◽  
Maria Gabriella Brasca ◽  
Antonella Ciavolella ◽  
Nicoletta Colombo ◽  
...  
Keyword(s):  
Cell Division ◽  
Kinase Inhibitors ◽  
Cell Division Cycle ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Cell Division Cycle 7

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
Sign in / Sign up

Export Citation Format

Share Document