Association of protein kinase A and protein phosphatase 2B with a common anchoring protein

Science ◽  
1995 ◽  
Vol 267 (5194) ◽  
pp. 108-111 ◽  
Author(s):  
V. Coghlan ◽  
B. Perrino ◽  
M Howard ◽  
L. Langeberg ◽  
J. Hicks ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2B ◽  
Anchoring Protein ◽  
Kinase A

Regulation of NF-κB activation by protein phosphatase 2B and NO, via protein kinase A activity, in human monocytes

Nitric Oxide ◽  
2003 ◽  
Vol 8 (1) ◽  
pp. 65-74 ◽  
Author(s):  
M Teresa Bengoechea-Alonso ◽  
Beatriz Pelacho ◽  
Juan A Osés-Prieto ◽  
Esteban Santiago ◽  
Natalia López-Moratalla ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Human Monocytes ◽  
Protein Phosphatase 2B ◽  
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

scholarly journals Protein Kinase A-induced tamoxifen resistance is mediated by anchoring protein AKAP13

BMC Cancer ◽  
2015 ◽  
Vol 15 (1) ◽  
Author(s):  
Cristiane Bentin Toaldo ◽  
Xanthippi Alexi ◽  
Karin Beelen ◽  
Marleen Kok ◽  
Michael Hauptmann ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Tamoxifen Resistance ◽  
Anchoring Protein ◽  
Kinase A

scholarly journals Radial Spoke Protein 3 Is a Mammalian Protein Kinase A-anchoring Protein That Binds ERK1/2

2009 ◽  
Vol 284 (43) ◽  
pp. 29437-29445 ◽  
Author(s):  
Arif Jivan ◽  
Svetlana Earnest ◽  
Yu-Chi Juang ◽  
Melanie H. Cobb
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Radial Spoke ◽  
Anchoring Protein ◽  
Mammalian Protein ◽  
Kinase A

Interaction Between Protein Kinase A (PKA) and Protein Phosphatase PP2A During Human Sperm Capacitation.

2012 ◽  
Vol 87 (Suppl_1) ◽  
pp. 448-448
Author(s):  
Patricio J. Morales ◽  
Kely Ordenes ◽  
Lidia Zuñiga ◽  
Emilce S. Diaz
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Human Sperm ◽  
Sperm Capacitation ◽  
Kinase A

scholarly journals Effects of protein phosphatase and kinase inhibitors on the cardiac L-type Ca current suggest two sites are phosphorylated by protein kinase A and another protein kinase.

1995 ◽  
Vol 106 (3) ◽  
pp. 393-414 ◽  
Author(s):  
H C Hartzell ◽  
Y Hirayama ◽  
J Petit-Jacques
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Phosphatase ◽  
Kinase Inhibitors ◽  
Delayed Rectifier ◽  
Internal Perfusion ◽  
Ca Current ◽  
Phosphatase Inhibitors ◽  
Pkc Inhibitors ◽  
Kinase A

We previously showed (Frace, A.M. and H.C. Hartzell. 1993. Journal of Physiology. 472:305-326) that internal perfusion of frog atrial myocytes with the nonselective protein phosphatase inhibitors microcystin or okadaic acid produced an increase in the L-type Ca current (ICa) and a decrease in the delayed rectifier K current (IK). We hypothesized that microcystin revealed the activity of a protein kinase (PKX) that was basally active in the cardiac myocyte that could phosphorylate the Ca and K channels or regulators of the channels. The present studies were aimed at determining the nature of PKX and its phosphorylation target. The effect of internal perfusion with microcystin on ICa or IK was not attenuated by inhibitors of protein kinase A (PKA). However, the effect of microcystin on ICa was largely blocked by the nonselective protein kinase inhibitors staurosporine (10-30 nM), K252a (250 nM), and H-7 (10 microM). Staurosporine and H-7 also decreased the stimulation of ICa by isoproterenol, but K252a was more selective and blocked the ability of microcystin to stimulate ICa without significantly reducing isoproterenol-stimulated current. Internal perfusion with selective inhibitors of protein kinase C (PKC), including the autoinhibitory pseudosubstrate PKC peptide (PKC(19-31)) and a myristoylated derivative of this peptide had no effect. External application of several PKC inhibitors had negative side effects that prevented their use as selective PKC inhibitors. Nevertheless, we conclude that PKX is not PKC. PKA and PKX phosphorylate sites with different sensitivities to the phosphatase inhibitors calyculin A and microcystin. In contrast to the results with ICa, the effect of microcystin on IK was not blocked by any of the kinase inhibitors tested, suggesting that the effect of microcystin on IK may not be mediated by a protein kinase but may be due to a direct effect of microcystin on the IK channel.

Sign in / Sign up

Export Citation Format

Share Document