scholarly journals Early glycogen synthase kinase‐3β and protein phosphatase 2A independent tau dephosphorylation during global brain ischaemia and reperfusion following cardiac arrest and the role of the adenosine monophosphate kinase pathway

2016 ◽  
Vol 44 (3) ◽  
pp. 1987-1997 ◽  
Author(s):  
Shohreh Majd ◽  
John H. T. Power ◽  
Simon A. Koblar ◽  
Hugh J. M. Grantham
Keyword(s):  
Protein Phosphatase ◽  
Glycogen Synthase ◽  
Adenosine Monophosphate ◽  
Brain Ischaemia ◽  
Ischaemia And Reperfusion ◽  
Phosphatase 2A ◽  
Global Brain Ischaemia ◽  
Global Brain ◽  
Kinase Pathway

scholarly journals HSP105 Recruits Protein Phosphatase 2A To Dephosphorylate β-Catenin

2015 ◽  
Vol 35 (8) ◽  
pp. 1390-1400 ◽  
Author(s):  
Nancy Yu ◽  
Michael Kakunda ◽  
Victoria Pham ◽  
Jennie R. Lill ◽  
Pan Du ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Target Gene ◽  
Target Genes ◽  
Glycogen Synthase ◽  
Protein Phosphatase 2A ◽  
Breast Cancer Patients ◽  
Poor Overall Survival ◽  
Protein Levels ◽  
Phosphatase 2A ◽  
Unidentified Component

The Wnt/β-catenin pathway causes accumulation of β-catenin in the cytoplasm and its subsequent translocation into the nucleus to initiate the transcription of the target genes. Without Wnt stimulation, β-catenin forms a complex with axin (axis inhibitor), adenomatous polyposis coli (APC), casein kinase 1α (CK1α), and glycogen synthase kinase 3β (GSK3β) and undergoes phosphorylation-dependent ubiquitination. Phosphatases, such as protein phosphatase 2A (PP2A), interestingly, also are components of this degradation complex; therefore, a balance must be reached between phosphorylation and dephosphorylation. How this balance is regulated is largely unknown. Here we show that a heat shock protein, HSP105, is a previously unidentified component of the β-catenin degradation complex. HSP105 is required for Wnt signaling, since depletion of HSP105 compromises β-catenin accumulation and target gene transcription upon Wnt stimulation. Mechanistically, HSP105 depletion disrupts the integration of PP2A into the β-catenin degradation complex, favoring the hyperphosphorylation and degradation of β-catenin. HSP105 is overexpressed in many types of tumors, correlating with increased nuclear β-catenin protein levels and Wnt target gene upregulation. Furthermore, overexpression of HSP105 is a prognostic biomarker that correlates with poor overall survival in breast cancer patients as well as melanoma patients participating in the BRIM2 clinical study.

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

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

scholarly journals Protein Phosphatase 2A Reactivates FOXO3a through a Dynamic Interplay with 14-3-3 and AKT

2010 ◽  
Vol 21 (6) ◽  
pp. 1140-1152 ◽  
Author(s):  
Amrik Singh ◽  
Min Ye ◽  
Octavian Bucur ◽  
Shudong Zhu ◽  
Maria Tanya Santos ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Transcriptional Activation ◽  
Protein Phosphatase ◽  
Nuclear Translocation ◽  
Akt Phosphorylation ◽  
Forkhead Box ◽  
Phosphatase 2A ◽  
And Function ◽  
Dynamic Interplay

Forkhead box transcription factor FOXO3a, a key regulator of cell survival, is regulated by reversible phosphorylation and subcellular localization. Although the kinases regulating FOXO3a activity have been characterized, the role of protein phosphatases (PP) in the control of FOXO3a subcellular localization and function is unknown. In this study, we detected a robust interaction between FOXO3a and PP2A. We further demonstrate that 14-3-3, while not impeding the interaction between PP2A and FOXO3a, restrains its activity toward AKT phosphorylation sites T32/S253. Disruption of PP2A function revealed that after AKT inhibition, PP2A-mediated dephosphorylation of T32/S253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of FOXO3a. Our findings reveal that distinct phosphatases dephosphorylate conserved AKT motifs within the FOXO family and that PP2A is entwined in a dynamic interplay with AKT and 14-3-3 to directly regulate FOXO3a subcellular localization and transcriptional activation.

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