scholarly journals Essential Role of Protein Phosphatase 2A in Metaphase II Arrest and Activation of Mouse Eggs Shown by Okadaic Acid, Dominant Negative Protein Phosphatase 2A, and FTY720

2011 ◽  
Vol 286 (16) ◽  
pp. 14705-14712 ◽  
Author(s):  
Heng-Yu Chang ◽  
Phoebe C. Jennings ◽  
Jessica Stewart ◽  
Nicole M. Verrills ◽  
Keith T. Jones
Keyword(s):  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Essential Role ◽  
Protein Phosphatase 2A ◽  
Dominant Negative ◽  
Phosphatase 2A ◽  
Mouse Eggs

scholarly journals Acute regulation of renal Na+/H+ exchanger NHE3 by dopamine: role of protein phosphatase 2A

2010 ◽  
Vol 298 (5) ◽  
pp. F1205-F1213 ◽  
Author(s):  
I. Alexandru Bobulescu ◽  
Henry Quiñones ◽  
Serge M. Gisler ◽  
Francesca Di Sole ◽  
Ming-Chang Hu ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Simian Virus 40 ◽  
Receptor Activation ◽  
T Antigen ◽  
Phosphatase 2A

Nephrogenic dopamine is a potent natriuretic paracrine/autocrine hormone that is central for mammalian sodium homeostasis. In the renal proximal tubule, dopamine induces natriuresis partly via inhibition of the sodium/proton exchanger NHE3. The signal transduction pathways and mechanisms by which dopamine inhibits NHE3 are complex and incompletely understood. This manuscript describes the role of the serine/threonine protein phosphatase 2A (PP2A) in the regulation of NHE3 by dopamine. The PP2A regulatory subunit B56δ (coded by the Ppp2r5d gene) directly associates with more than one region of the carboxy-terminal hydrophilic putative cytoplasmic domain of NHE3 (NHE3-cyto), as demonstrated by yeast-two-hybrid, coimmunoprecipitation, blot overlay, and in vitro pull-down assays. Phosphorylated NHE3-cyto is a substrate for purified PP2A in an in vitro dephosphorylation reaction. In cultured renal cells, inhibition of PP2A by either okadaic acid or by overexpression of the simian virus 40 (SV40) small T antigen blocks the ability of dopamine to inhibit NHE3 activity and to reduce surface NHE3 protein. Dopamine-induced NHE3 redistribution is also blocked by okadaic acid ex vivo in rat kidney cortical slices. These studies demonstrate that PP2A is an integral and critical participant in the signal transduction pathway between dopamine receptor activation and NHE3 inhibition.

2214 Role of protein phosphatase 2A in hippocampal long-term potentiation

1997 ◽  
Vol 28 ◽  
pp. S254
Author(s):  
Kohji Fukunaga ◽  
Dominique Muller ◽  
Masao Ohmitsu ◽  
Eishichi Miyamoto
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Long Term Potentiation ◽  
Term Potentiation ◽  
Phosphatase 2A

scholarly journals Role of Protein Phosphatase 2A in Regulating the Visual Signaling in Drosophila

2008 ◽  
Vol 28 (6) ◽  
pp. 1444-1451 ◽  
Author(s):  
N. Wang ◽  
H.-T. Leung ◽  
W. L. Pak ◽  
Y. T. Carl ◽  
B. E. Wadzinski ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Visual Signaling ◽  
Phosphatase 2A

Propofol Inhibits Phosphorylation of N -methyl-d-aspartate Receptor NR1 Subunits in Neurons

2006 ◽  
Vol 104 (4) ◽  
pp. 763-769 ◽  
Author(s):  
Seth Kingston ◽  
Limin Mao ◽  
Lu Yang ◽  
Anish Arora ◽  
Eugene E. Fibuch ◽  
...  
Keyword(s):  
Glutamate Receptors ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Cortical Neurons ◽  
Protein Phosphatase 2A ◽  
Ionotropic Glutamate Receptors ◽  
Dependent Manner ◽  
Calyculin A ◽  
General Anesthetic ◽  
Phosphatase 2A

Background Anesthetics may interact with ionotropic glutamate receptors to produce some of their biologic actions. Cellular studies reveal that the ionotropic glutamate receptors, N-methyl-D-aspartate receptors (NMDARs), can be phosphorylated on their NR1 subunits at the C-terminal serine residues, which is a major mechanism for the regulation of NMDAR functions. It is currently unknown whether anesthetics have any modulatory effects on NMDAR NR1 subunit phosphorylation. Methods The possible effect of a general anesthetic propofol on phosphorylation of NR1 subunits at serine 897 (pNR1S897) and 896 (pNR1S896) was detected in cultured rat cortical neurons. Results Propofol consistently reduced basal levels of pNR1S897 and pNR1S896 in a concentration-dependent manner. This reduction was rapid as the reliable reduction of pNR1S896 developed 1 min after propofol administration. Pretreatment of cultures with the protein phosphatase 2A inhibitors okadaic acid or calyculin A blocked the effect of propofol on the NR1 phosphorylation, whereas okadaic acid or calyculin A alone did not alter basal pNR1S897 and pNR1S896 levels. In addition, propofol decreased tyrosine phosphorylation of protein phosphatase 2A at tyrosine 307, resulting in an increase in protein phosphatase 2A activity. In the presence of propofol, the NMDAR agonist-induced intracellular Ca2+ increase was impaired in neurons with dephosphorylated NR1 subunits. Conclusions Together, these data indicate an inhibitory effect of a general anesthetic propofol on NMDAR NR1 subunit phosphorylation in neurons. This inhibition was mediated through a signaling mechanism involving activation of protein phosphatase 2A.

Protein Phosphatase 2A Inactivates Bcl2’s Antiapoptotic Function by Dephosphorylation and Up-Regulation of Bcl2-p53 Binding.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1436-1436
Author(s):  
Xingming Deng ◽  
Fengqin Gao ◽  
Tammy Flagg ◽  
W. Stratford May
Keyword(s):  
Cell Death ◽  
Cell Survival ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Apoptotic Cell ◽  
Protein Phosphatase 2A ◽  
Survival Function ◽  
Phosphorylation Site ◽  
Apoptotic Cell Death ◽  
Phosphatase 2A

Abstract DNA damage-induced p53/Bcl2 interaction at the outer mitochondrial membranes results in a Bcl2 conformational change and loss of its antiapoptotic function. Our data now indicate that either treatment of cells with the protein phosphatase 2A (PP2A) inhibitor, okadaic acid (10 nM), or specific disruption of PP2A activity by the expression of SV40 small tumor antigen enhances Bcl2 phosphorylation and suppresses the cisplatin-stimulated Bcl2-p53 interaction in association with prolonged cell survival. By contrast, C2-ceramide, a potent PP2A activator, reduces Bcl2 phosphorylation and increases Bcl2-p53 binding and promotes apoptotic cell death, suggesting that PP2A may function as a physiological regulator of Bcl2 by, at least in part, affecting its association with p53. Overexpression of the PP2A catalytic subunit (PP2A/C) suppresses Bcl2 phosphorylation in association with increased p53-Bcl2 binding and apoptotic cell death. By contrast, specific depletion of PP2A/C by RNA interference enhances Bcl2 phosphorylation, suppresses p53-Bcl2 interaction and prolongs cell survival. Purified PP2A can directly enhance the formation of the p53-Bcl2 complex in vitro in an okadaic acid-sensitive manner, supporting a direct mechanism. Importantly, PP2A directly interacts with Bcl2 at its BH4 domain which may function as the PP2A ‘docking site’ to potentially ‘bridge’ PP2A to the flexible loop domain which contains the physiological serine 70 phosphorylation site. Thus, PP2A may provide a double whammy to Bcl2’s survival function by both dephosphorylating and enhancing p53-Bcl2 binding. Therapeutically stimulating Bcl2 dephosphorylation and/or increasing Bcl2/p53 binding by activating PP2A may represent an efficient and novel antineoplastic approach.

scholarly journals Role of Protein Phosphatase 2A in mGluR5-regulated MEK/ERK Phosphorylation in Neurons

2005 ◽  
Vol 280 (13) ◽  
pp. 12602-12610 ◽  
Author(s):  
Limin Mao ◽  
Lu Yang ◽  
Anish Arora ◽  
Eun Sang Choe ◽  
Guochi Zhang ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Erk Phosphorylation ◽  
Phosphatase 2A

The role of subunit B’ of protein phosphatase 2A in pathogenesis of Heterodera schachtii on Arabidopsis thaliana roots

2016 ◽  
Vol 33 ◽  
pp. S157
Author(s):  
Dominik Kanigowski ◽  
Mateusz Matuszkiewicz ◽  
Joanna Dąbrowska ◽  
Anna Barczak ◽  
Marcin Filipecki
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Heterodera Schachtii ◽  
Phosphatase 2A ◽  
Subunit B
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