scholarly journals Integrin Cross-talk in Endothelial Cells Is Regulated by Protein Kinase A and Protein Phosphatase 1

2008 ◽  
Vol 283 (46) ◽  
pp. 31849-31860 ◽  
Author(s):  
Annette M. Gonzalez ◽  
Jessica Claiborne ◽  
Jonathan C. R. Jones
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Cross Talk ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Kinase A

scholarly journals Full activation of a nuclear species of protein phosphatase-1 by phosphorylation with protein kinase A and casein kinase-2

1994 ◽  
Vol 297 (3) ◽  
pp. 447-449 ◽  
Author(s):  
A Van Eynde ◽  
M Beullens ◽  
W Stalmans ◽  
M Bollen
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Fold Increase ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Catalytic Subunit ◽  
Protein Phosphatase 1 ◽  
Nuclear Species ◽  
Kinase A

Bovine thymus nuclei contain a species of protein phosphatase-1 (PP-1N alpha) that can be partially activated by phosphorylation of an associated inhibitory polypeptide, NIPP-1, with protein kinase A [Beullens, Van Eynde, Bollen and Stalmans (1993) J. Biol. Chem. 268, 13172-13177]. Here it is shown that PP-1N alpha can also be activated 4-fold by phosphorylation of NIPP-1 with casein kinase-2. The effects of protein kinase A and casein kinase-2 were additive, yielding an enzyme with an activity close to that of the free catalytic subunit. Casein kinase-2 introduced up to 1.2 phosphate groups into purified NIPP-1 on serine and threonine residues. This phosphorylation was associated with a 14-fold increase in the concentration of NIPP-1 required for 50% inhibition of the type-1 catalytic subunit. The kinase-mediated inactivation of NIPP-1 could be reversed by incubation with the catalytic subunit of protein phosphatase-2A.

Mn2+-dependent protein phosphatase 1 enhances protein kinase A-induced Ca2+ desensitisation in skinned murine myocardium

2007 ◽  
Vol 74 (1) ◽  
pp. 124-132 ◽  
Author(s):  
A NEULEN ◽  
N BLAUDECK ◽  
S ZITTRICH ◽  
D METZLER ◽  
G PFITZER ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Dependent Protein ◽  
Kinase A

scholarly journals A refractory phase in cyclic AMP-responsive transcription requires down regulation of protein kinase A.

1995 ◽  
Vol 15 (3) ◽  
pp. 1826-1832 ◽  
Author(s):  
R Armstrong ◽  
W Wen ◽  
J Meinkoth ◽  
S Taylor ◽  
M Montminy
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Refractory Period ◽  
Protein Phosphatase 1 ◽  
Creb Phosphorylation ◽  
Subunit Expression ◽  
C Subunit ◽  
Kinase A

Cyclic AMP (cAMP) stimulates the expression of numerous genes through the protein kinase A (PK-A)-mediated phosphorylation of the nuclear factor CREB at Ser-133 (G. A. Gonzalez and M. R. Montminy, Cell 59:675-680, 1989). Like other signal transduction pathways, cAMP induces gene expression with burst-attenuation kinetics; cAMP-dependent transcription and CREB phosphorylation peak within 30 min and decline steadily over the next 4 to 6 h via the protein phosphatase 1-mediated dephosphorylation of CREB (M. Hagiwara, A. Alberts, P. Brindle, J. Meinkoth, J. Feramisco, T. Deng, M. Karin, S. Shenolikar, and M. Montminy, Cell 70:105-113, 1992). Here we characterize a third phase in cAMP-responsive transcription--a refractory period during which hormone-treated cells become transcriptionally unresponsive to subsequent stimulation by cAMP. This refractory period begins 6 to 8 h after stimulation and lasts 3 to 5 days after the removal of hormone. In contrast to the earlier attenuation phase, transcription of cAMP-responsive genes during the refractory period is not restored by inhibitors of protein phosphatase 1 activity. Rather, the establishment and maintenance of this phase rely on a marked reduction in PK-A catalytic subunit expression at the translational level. As overexpression of C-subunit protein can reactive transcription of cAMP-responsive genes during the refractory period, our results suggest that hormone-responsive cells may stimulate, attenuate, and then silence signal-dependent genes through distinct regulatory mechanisms.

scholarly journals Characterization of a Novel Chemokine-Containing Storage Granule in Endothelial Cells: Evidence for Preferential Exocytosis Mediated by Protein Kinase A and Diacylglycerol

2005 ◽  
Vol 175 (8) ◽  
pp. 5358-5369 ◽  
Author(s):  
Inger Øynebråten ◽  
Nicolas Barois ◽  
Kathrine Hagelsteen ◽  
Finn-Eirik Johansen ◽  
Oddmund Bakke ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Storage Granule ◽  
Kinase A

scholarly journals Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56  subunit

2007 ◽  
Vol 104 (8) ◽  
pp. 2979-2984 ◽  
Author(s):  
J.-H. Ahn ◽  
T. McAvoy ◽  
S. V. Rakhilin ◽  
A. Nishi ◽  
P. Greengard ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A ◽  
Kinase A
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