Ca2+/Calmodulin Activates an MAP Kinase Through the Inhibition of a Protein Phosphatase (DsPTP1) in Arabidopsis

2021 ◽  
Author(s):  
Kyung Eun Kim ◽  
Nhan Thi Nguyen ◽  
Sun Ho Kim ◽  
Sunghwa Bahk ◽  
Mi Sun Cheong ◽  
...  
Keyword(s):  
Map Kinase ◽  
Protein Phosphatase

scholarly journals Mitogen-Activated Protein Kinase and Cell Cycle Progression During Mouse Egg Activation Induced by Various Stimuli

1999 ◽  
Vol 54 (3-4) ◽  
pp. 285-294 ◽  
Author(s):  
Q. Y. Sun ◽  
Y. Lax ◽  
S. Rubinstein ◽  
D. Y. Chen ◽  
H. Breitbart
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Protein Phosphatase ◽  
Kinase Activity ◽  
Polar Body ◽  
Sperm Chromatin ◽  
Mitogen Activated Protein ◽  
Second Polar Body ◽  
Pronuclear Formation ◽  
Mouse Egg

Abstract A very sensitive method was established for detecting the activity of mitogen-activated protein (MAP) kinase in mouse eggs, and used to follow temporal changes of this kinase during fertilization and sponatenous or chemically-induced parthenogenic activation. MAP kinase activity increased between 1 and 2.5 h post-insemination, at which time the second polar body was emitted and sperm chromatin was dispersed; its activity decreased sharply at 8 h, when pronuclei were formed. Both calcium ionophore A23187 and ethanol simulta­ neously induced pronuclear formation and MAP kinase inactivation in aged eggs 8 h after incubation but less effectively in fresh eggs. The protein kinase inhibitor staurosporine in­duced pronuclear formation and MAP kinase inactivation more quickly than other treat­ ments, with MAP kinase inactivation occurring slightly proceeding pronuclear formation. Okadaic acid, a specific inhibitor of protein phosphatase 1 and 2A , induced increase in MAP kinase activity, and overcame pronuclear formation induced by various stimuli. MAP kinase inactivation preceded pronuclear formation in eggs spontaneously activated by aging in vitro, perhaps due to cytoplasmic degeneration and thus delayed response of nuclear envelope precursors to MAP kinase inactivation. These data suggest that MAP kinase is a key protein kinase regulating the events of mouse egg activation. Increased MAP kinase activity is temporally correlated with the second polar body emission and sperm chromatin decondensation. Although different stimuli (including sperm) may initially act through different mechanisms, they finally inactivate MAP kinase, probably by allowing the action of protein phosphatase, and thus induces the transition to interphase.

scholarly journals The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf

1994 ◽  
Vol 303 (1) ◽  
pp. 21-26 ◽  
Author(s):  
D A E Cross ◽  
D R Alessi ◽  
J R Vandenheede ◽  
H E McDowell ◽  
H S Hundal ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Map Kinase ◽  
Protein Phosphatase ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase 3 ◽  
Rat Skeletal Muscle ◽  
S6 Kinase ◽  
P70 S6 Kinase ◽  
Skeletal Muscle Cell Line ◽  
Stimulation Of

Glycogen synthase kinase-3 (GSK3) is inactivated in vitro by p70 S6 kinase or MAP kinase-activated protein kinase-1 beta (MAPKAP kinase-1 beta; also known as Rsk-2). Here we show that GSK3 isoforms are inhibited by 40% within minutes after stimulation of the rat skeletal-muscle cell line L6 with insulin-like growth factor-1 (IGF-1) or insulin. GSK3 was similarly inhibited in rabbit skeletal muscle after an intravenous injection of insulin. Inhibition resulted from increased phosphorylation of GSK3, probably at a serine/threonine residue(s), because it was reversed by incubation with protein phosphatase-2A. Rapamycin blocked the activation of p70 S6 kinase by IGF-1 in L6 cells, but had no effect on the inhibition of GSK3 or the activation of MAPKAP kinase-1 beta. In contrast, wortmannin, a potent inhibitor of PtdIns 3-kinase, prevented the inactivation of GSK3 and the activation of MAPKAP kinase-1 beta and p70 S6 kinase by IGF-1 or insulin. Wortmannin also blocked the activation of p74raf-1. MAP kinase kinase and p42 MAP kinase, but not the formation of GTP-Ras by IGF-1. The results suggest that the stimulation of glycogen synthase by insulin/IGF-1 in skeletal muscle involves the MAP-KAP kinase-1-catalysed inhibition of GSK3, as well as the previously described activation of the glycogen-associated form of protein phosphatase-1.

Inhibition of protein phosphatase methylesterase 1 dysregulates MAP kinase signaling and attenuates muscle cell differentiation

Gene ◽  
2020 ◽  
Vol 739 ◽  
pp. 144515 ◽  
Author(s):  
Sydney A. Labuzan ◽  
Sarah A. Lynch ◽  
Lisa M. Cooper ◽  
David S. Waddell
Keyword(s):  
Cell Differentiation ◽  
Map Kinase ◽  
Muscle Cell ◽  
Protein Phosphatase ◽  
Kinase Signaling ◽  
Muscle Cell Differentiation ◽  
Map Kinase Signaling

Antagonistic interaction between MAP kinase and protein phosphatase 2C in stress recovery

Plant Science ◽  
2006 ◽  
Vol 171 (5) ◽  
pp. 596-606 ◽  
Author(s):  
Jeffrey Leung ◽  
Sofia Orfanidi ◽  
Françoise Chefdor ◽  
Tamás Mészaros ◽  
Susanne Bolte ◽  
...  
Keyword(s):  
Map Kinase ◽  
Protein Phosphatase ◽  
Stress Recovery ◽  
Protein Phosphatase 2C ◽  
Antagonistic Interaction

CK2α — protein phosphatase 2A molecular complex: Possible interaction with the MAP kinase pathway

1999 ◽  
pp. 207-212
Author(s):  
Franck Lebrin ◽  
Laurence Bianchini ◽  
Thierry Rabilloud ◽  
Edmond M. Chambaz ◽  
Yves Goldberg
Keyword(s):  
Map Kinase ◽  
Molecular Complex ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A ◽  
Map Kinase Pathway ◽  
Kinase Pathway
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