Characterization of a cDNA encoding the 55 kDa B regulatory subunit of Arabidopsis protein phosphatase 2A

1995 ◽  
Vol 28 (2) ◽  
pp. 257-266 ◽  
Author(s):  
Sabine J. Rundle ◽  
Andrew J. Hartung ◽  
John W. Corum ◽  
Michael O'Neill
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Arabidopsis Protein ◽  
Phosphatase 2A

Molecular characterization of the B' regulatory subunit gene family of Arabidopsis protein phosphatase 2A

1999 ◽  
Vol 260 (1) ◽  
pp. 127-136 ◽  
Author(s):  
J. Georgia Haynes ◽  
Andrew J. Hartung ◽  
John D. Hendershot ◽  
R. Scott Passingham ◽  
Sabine J. Rundle
Keyword(s):  
Gene Family ◽  
Molecular Characterization ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Subunit Gene ◽  
Arabidopsis Protein ◽  
Phosphatase 2A

scholarly journals Cloning and characterization of Bδ, a novel regulatory subunit of protein phosphatase 2A

FEBS Letters ◽  
1999 ◽  
Vol 460 (3) ◽  
pp. 462-466 ◽  
Author(s):  
Stefan Strack ◽  
Dennis Chang ◽  
Julie A. Zaucha ◽  
Roger J. Colbran ◽  
Brian E. Wadzinski
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Phosphatase 2A

scholarly journals Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A.

1994 ◽  
Vol 269 (22) ◽  
pp. 15668-15675 ◽  
Author(s):  
X. Cayla ◽  
C. Van Hoof ◽  
M. Bosch ◽  
E. Waelkens ◽  
J. Vandekerckhove ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A

scholarly journals Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing

1993 ◽  
Vol 268 (20) ◽  
pp. 15267-15276
Author(s):  
P. Hendrix ◽  
R.E. Mayer-Jackel ◽  
P. Cron ◽  
J. Goris ◽  
J. Hofsteenge ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Phosphatase 2A

scholarly journals Regulatory Subunit B′γ of Protein Phosphatase 2A Prevents Unnecessary Defense Reactions under Low Light in Arabidopsis

2011 ◽  
Vol 156 (3) ◽  
pp. 1464-1480 ◽  
Author(s):  
Andrea Trotta ◽  
Michael Wrzaczek ◽  
Judith Scharte ◽  
Mikko Tikkanen ◽  
Grzegorz Konert ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Low Light ◽  
Defense Reactions ◽  
Phosphatase 2A ◽  
Subunit B

scholarly journals Protein Phosphatase 2A Regulatory Subunit B56α Associates with c-Myc and Negatively Regulates c-Myc Accumulation

2006 ◽  
Vol 26 (7) ◽  
pp. 2832-2844 ◽  
Author(s):  
Hugh K. Arnold ◽  
Rosalie C. Sears
Keyword(s):  
Tumor Suppressor ◽  
Protein Phosphatase ◽  
Cell Function ◽  
Cell Transformation ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Suppressor Activity ◽  
Tumor Suppressor Activity ◽  
Structural Subunit ◽  
Phosphatase 2A

ABSTRACT Protein phosphatase 2A (PP2A) plays a prominent role in controlling accumulation of the proto-oncoprotein c-Myc. PP2A mediates its effects on c-Myc by dephosphorylating a conserved residue that normally stabilizes c-Myc, and in this way, PP2A enhances c-Myc ubiquitin-mediated degradation. Stringent regulation of c-Myc levels is essential for normal cell function, as c-Myc overexpression can lead to cell transformation. Conversely, PP2A has tumor suppressor activity. Uncovering relevant PP2A holoenzymes for a particular target has been limited by the fact that cellular PP2A represents a large heterogeneous population of trimeric holoenzymes, composed of a conserved catalytic subunit and a structural subunit along with a variable regulatory subunit which directs the holoenzyme to a specific target. We now report the identification of a specific PP2A regulatory subunit, B56α, that selectively associates with the N terminus of c-Myc. B56α directs intact PP2A holoenzymes to c-Myc, resulting in a dramatic reduction in c-Myc levels. Inhibition of PP2A-B56α holoenzymes, using small hairpin RNA to knock down B56α, results in c-Myc overexpression, elevated levels of c-Myc serine 62 phosphorylation, and increased c-Myc function. These results uncover a new protein involved in regulating c-Myc expression and reveal a critical interconnection between a potent oncoprotein, c-Myc, and a well-documented tumor suppressor, PP2A.

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