scholarly journals Assays for Chemotaxis and Chemoattractant-Stimulated TorC2 Activation and PKB Substrate Phosphorylation in Dictyostelium

2009 ◽  
pp. 255-270 ◽  
Author(s):  
Yoichiro Kamimura ◽  
Ming Tang ◽  
Peter Devreotes
Keyword(s):  
Substrate Phosphorylation

Insulin-receptor autophosphorylation and endogenous substrate phosphorylation in human adipocytes from control, obese, and NIDDM subjects

Diabetes ◽  
1990 ◽  
Vol 39 (2) ◽  
pp. 250-259 ◽  
Author(s):  
R. S. Thies ◽  
J. M. Molina ◽  
T. P. Ciaraldi ◽  
G. R. Freidenberg ◽  
J. M. Olefsky
Keyword(s):  
Insulin Receptor ◽  
Human Adipocytes ◽  
Endogenous Substrate ◽  
Substrate Phosphorylation

scholarly journals Substrate Phosphorylation Catalyzed by the Insulin Receptor Tyrosine Kinase

1989 ◽  
Vol 264 (36) ◽  
pp. 21557-21572
Author(s):  
J R Flores-Riveros ◽  
E Sibley ◽  
T Kastelic ◽  
M D Lane
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Substrate Phosphorylation

scholarly journals Substrate phosphorylation specificity of the human c-kit receptor tyrosine kinase.

1991 ◽  
Vol 266 (30) ◽  
pp. 19908-19916 ◽  
Author(s):  
R. Herbst ◽  
R. Lammers ◽  
J. Schlessinger ◽  
A. Ullrich
Keyword(s):  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kit Receptor ◽  
Substrate Phosphorylation

scholarly journals Budding yeast relies on G1 cyclin specificity to couple cell cycle progression with morphogenetic development

2021 ◽  
Vol 7 (23) ◽  
pp. eabg0007
Author(s):  
Deniz Pirincci Ercan ◽  
Florine Chrétien ◽  
Probir Chakravarty ◽  
Helen R. Flynn ◽  
Ambrosius P. Snijders ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Budding Yeast ◽  
Quantitative Model ◽  
Cyclin Dependent Kinase ◽  
Cycle Progression ◽  
Model Cell ◽  
Mitotic Cyclin ◽  
Substrate Phosphorylation ◽  
The Cost

Two models have been put forward for cyclin-dependent kinase (Cdk) control of the cell cycle. In the qualitative model, cell cycle events are ordered by distinct substrate specificities of successive cyclin waves. Alternatively, in the quantitative model, the gradual rise of Cdk activity from G1 phase to mitosis leads to ordered substrate phosphorylation at sequential thresholds. Here, we study the relative contributions of qualitative and quantitative Cdk control in Saccharomyces cerevisiae. All S phase and mitotic cyclins can be replaced by a single mitotic cyclin, albeit at the cost of reduced fitness. A single cyclin can also replace all G1 cyclins to support ordered cell cycle progression, fulfilling key predictions of the quantitative model. However, single-cyclin cells fail to polarize or grow buds and thus cannot survive. Our results suggest that budding yeast has become dependent on G1 cyclin specificity to couple cell cycle progression to essential morphogenetic events.

N-methyl-d-aspartate-induced long-term depression is associated with a decrease in postsynaptic protein kinase C substrate phosphorylation in rat hippocampal slices

2002 ◽  
Vol 320 (3) ◽  
pp. 129-132 ◽  
Author(s):  
Els J.M. van Dam ◽  
Bert Ruiter ◽  
Amer Kamal ◽  
Geert M.J. Ramakers ◽  
Willem Hendrik Gispen ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Hippocampal Slices ◽  
Long Term Depression ◽  
Postsynaptic Protein ◽  
Kinase C ◽  
Substrate Phosphorylation

scholarly journals Activation State-Dependent Substrate Gating in Ca2+/Calmodulin-Dependent Protein Kinase II

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
D. E. Johnson ◽  
A. Hudmon
Keyword(s):  
Protein Kinase ◽  
Catalytic Domain ◽  
Intrinsic Property ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
State Dependent ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Substrate Phosphorylation ◽  
The Brain

Calcium/calmodulin-dependent protein kinase II (CaMKII) is highly concentrated in the brain where its activation by the Ca2+sensor CaM, multivalent structure, and complex autoregulatory features make it an ideal translator of Ca2+signals created by different patterns of neuronal activity. We provide direct evidence that graded levels of kinase activity and extent of T287(T286αisoform) autophosphorylation drive changes in catalytic output and substrate selectivity. The catalytic domains of CaMKII phosphorylate purified PSDs much more effectively when tethered together in the holoenzyme versus individual subunits. Using multisubstrate SPOT arrays, high-affinity substrates are preferentially phosphorylated with limited subunit activity per holoenzyme, whereas multiple subunits or maximal subunit activation is required for intermediate- and low-affinity, weak substrates, respectively. Using a monomeric form of CaMKII to control T287autophosphorylation, we demonstrate that increased Ca2+/CaM-dependent activity for all substrates tested, with the extent of weak, low-affinity substrate phosphorylation governed by the extent of T287autophosphorylation. Our data suggest T287autophosphorylation regulates substrate gating, an intrinsic property of the catalytic domain, which is amplified within the multivalent architecture of the CaMKII holoenzyme.

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