ChemInform Abstract: Benzo(c)quinoliziniums: A New Family of Inhibitors for Protein Kinase CKII

ChemInform ◽  
2010 ◽  
Vol 28 (35) ◽  
pp. no-no
Author(s):  
Y. METTEY ◽  
J.-M. VIERFOND ◽  
M. BAUDRY ◽  
C. COCHET ◽  
D. SARROUILHE
2000 ◽  
Vol 351 (1) ◽  
pp. 143-150 ◽  
Author(s):  
Gian Luigi RUSSO ◽  
Christian VAN DEN BOS ◽  
Ann SUTTON ◽  
Paola COCCETTI ◽  
Maurizio D. BARONI ◽  
...  

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.


1999 ◽  
Vol 263 (3) ◽  
pp. 743-748 ◽  
Author(s):  
Mi-Young Son ◽  
Jang-Woon Park ◽  
Yun-Sook Kim ◽  
Sek-Won Kang ◽  
Daniel R. Marshak ◽  
...  

2018 ◽  
Vol 29 (17) ◽  
pp. 2128-2136 ◽  
Author(s):  
Françoise M. Roelants ◽  
Neha Chauhan ◽  
Alexander Muir ◽  
Jameson C. Davis ◽  
Anant K. Menon ◽  
...  

In our proteome-wide screen, Ysp2 (also known as Lam2/Ltc4) was identified as a likely physiologically relevant target of the TOR complex 2 (TORC2)–dependent protein kinase Ypk1 in the yeast Saccharomyces cerevisiae. Ysp2 was subsequently shown to be one of a new family of sterol-binding proteins located at plasma membrane (PM)–endoplasmic reticulum (ER) contact sites. Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER. Furthermore, we provide evidence that a change in PM sterol homeostasis promotes cell survival under membrane-perturbing conditions known to activate TORC2-Ypk1 signaling. These observations define the underlying molecular basis of a new regulatory mechanism for cellular response to plasma membrane stress.


2002 ◽  
Vol 278 (5) ◽  
pp. 2829-2836 ◽  
Author(s):  
Sricharan Bandhakavi ◽  
Richard O. McCann ◽  
David E. Hanna ◽  
Claiborne V. C. Glover

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