scholarly journals Protein phosphatase 2A (PP2A) regulatory subunit B′γ interacts with cytoplasmic ACONITASE 3 and modulates the abundance of AOX1A and AOX1D inArabidopsis thaliana

2014 ◽  
Vol 205 (3) ◽  
pp. 1250-1263 ◽  
Author(s):  
Grzegorz Konert ◽  
Andrea Trotta ◽  
Petri Kouvonen ◽  
Moona Rahikainen ◽  
Guido Durian ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Phosphatase 2A ◽  
Subunit B

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 Molecular cloning of a 74-kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A

FEBS Letters ◽  
1996 ◽  
Vol 379 (1) ◽  
pp. 107-111 ◽  
Author(s):  
Osamu Tanabe ◽  
Terumasa Nagase ◽  
Takehiko Murakami ◽  
Hideto Nozaki ◽  
Hirofumi Usui ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Human Protein ◽  
Regulatory Subunit ◽  
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.

scholarly journals Cdc55p, the B-type regulatory subunit of protein phosphatase 2A, has multiple functions in mitosis and is required for the kinetochore/spindle checkpoint in Saccharomyces cerevisiae.

1997 ◽  
Vol 17 (2) ◽  
pp. 620-626 ◽  
Author(s):  
Y Wang ◽  
D J Burke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Elevated Temperatures ◽  
Protein Phosphatase 2A ◽  
Spindle Checkpoint ◽  
Mitotic Checkpoint ◽  
Regulatory Subunit ◽  
Phosphatase 2A ◽  
A Subunit ◽  
Normal Sensitivity

Saccharomyces cerevisiae, like most eucaryotic cells, can prevent the onset of anaphase until chromosomes are properly aligned on the mitotic spindle. We determined that Cdc55p (regulatory B subunit of protein phosphatase 2A [PP2A]) is required for the kinetochore/spindle checkpoint regulatory pathway in yeast. ctf13 cdc55 double mutants could not maintain a ctf13-induced mitotic delay, as determined by antitubulin staining and levels of histone H1 kinase activity. In addition, cdc55::LEU2 mutants and tpd3::LEU2 mutants (regulatory A subunit of PP2A) were nocodazole sensitive and exhibited the phenotypes of previously identified kinetochore/spindle checkpoint mutants. Inactivating CDC55 did not simply bypass the arrest that results from inhibiting ubiquitin-dependent proteolysis because cdc16-1 cdc55::LEU2 and cdc23-1 cdc55::LEU2 double mutants arrested normally at elevated temperatures. CDC55 is specific for the kinetochore/spindle checkpoint because cdc55 mutants showed normal sensitivity to gamma radiation and hydroxyurea. The conditional lethality and the abnormal cellular morphogenesis of cdc55::LEU2 were suppressed by cdc28F19, suggesting that the cdc55 phenotypes are dependent on the phosphorylation state of Cdc28p. In contrast, the nocodazole sensitivity of cdc55::LEU2 was not suppressed by cdc28F19. Therefore, the mitotic checkpoint activity of CDC55 (and TPD3) is independent of regulated phosphorylation of Cdc28p. Finally, cdc55::LEU2 suppresses the temperature sensitivity of cdc20-1, suggesting additional roles for CDC55 in mitosis.

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