Genomic Organisation, Chromosomal Localisation Tissue Distribution and Developmental Regulation of the PR61/B′ Regulatory Subunits of Protein Phosphatase 2A in Mice

2004 ◽  
Vol 336 (4) ◽  
pp. 971-986 ◽  
Author(s):  
Ellen Martens ◽  
Ilse Stevens ◽  
Veerle Janssens ◽  
Joris Vermeesch ◽  
Jürgen Götz ◽  
...  
2002 ◽  
Vol 16 (11) ◽  
pp. 2039-2048 ◽  
Author(s):  
Karsten Schmidt ◽  
Stefan Kins ◽  
Andreas Schild ◽  
Roger M. Nitsch ◽  
Brian A. Hemmings ◽  
...  

2001 ◽  
Vol 353 (3) ◽  
pp. 417-439 ◽  
Author(s):  
Veerle JANSSENS ◽  
Jozef GORIS

Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate specificity, (sub)cellular localization and catalytic activity of the PP2A holoenzymes. Moreover, the catalytic subunit is subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices. The regulatory ability of PTPA (PTPase activator), originally identified as a protein stimulating the phosphotyrosine phosphatase activity of PP2A, will also be discussed, alongside the other regulatory inputs. The use of specific PP2A inhibitors and molecular genetics in yeast, Drosophila and mice has revealed roles for PP2A in cell cycle regulation, cell morphology and development. PP2A also plays a prominent role in the regulation of specific signal transduction cascades, as witnessed by its presence in a number of macromolecular signalling modules, where it is often found in association with other phosphatases and kinases. Additionally, PP2A interacts with a substantial number of other cellular and viral proteins, which are PP2A substrates, target PP2A to different subcellular compartments or affect enzyme activity. Finally, the de-regulation of PP2A in some specific pathologies will be touched upon.


PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e67987 ◽  
Author(s):  
Behzad Heidari ◽  
Dugassa Nemie-Feyissa ◽  
Saijaliisa Kangasjärvi ◽  
Cathrine Lillo

2011 ◽  
Vol 156 (1) ◽  
pp. 165-172 ◽  
Author(s):  
Behzad Heidari ◽  
Polina Matre ◽  
Dugassa Nemie-Feyissa ◽  
Christian Meyer ◽  
Odd Arne Rognli ◽  
...  

2013 ◽  
Vol 14 (5) ◽  
pp. 518-529 ◽  
Author(s):  
Joon-Hee Shin ◽  
Jung-Eun Kim ◽  
Martha Malapi-Wight ◽  
Yoon-E. Choi ◽  
Brian D. Shaw ◽  
...  

1999 ◽  
Vol 380 (9) ◽  
pp. 1117-1120 ◽  
Author(s):  
Jürgen Götz ◽  
Wilfried Kues

AbstractProtein phosphatase 2A (PP2A) constitutes one of the major families of protein serine/threonine phosphatases found in all eukaryotic cells. PP2A holoenzymes are composed of a catalytic subunit complexed with a structural regulatory subunit of 65 kDa. These core subunits associate with regulatory subunits of various sizes to form different heterotrimers which have been purified and evaluated with regard to substrate specificity. In fully differentiated tissues PP2A expression levels are highest in the brain, however, relatively little is known about expression in the developing embryo.In order to determine the composition of PP2A catalytic subunits in the mouse, cDNAs were cloned and the genomic organization of PP2A Cα was determined.By a gene targeting approach in the mouse, we have previously shown that the absence of the major catalytic subunit of PP2A, Cα, resulted in embryonic lethality around embryonic day E6.5. No mesoderm was formed which implied that PP2A plays a crucial role in gastrulation.Here, we extended our studies and analyzed wildtype embryos for Cα expression at subsequent stages of development. After gastrulation is completed, we find high expression of Cα restricted to the neural folds, which suggests that PP2A plays an additional pivotal role in neurulation.


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