scholarly journals Purification and characterization of an autophosphorylation-activated protein serine threonine kinase that phosphorylates and inactivates protein phosphatase 2A

1993 ◽  
Vol 268 (15) ◽  
pp. 11193-11198 ◽  
Author(s):  
H. Guo ◽  
S.A. Reddy ◽  
Z. Damuni
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Purification And Characterization ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Phosphatase 2A

scholarly journals ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase)

2017 ◽  
Vol 37 (10) ◽  
pp. 2709-2722 ◽  
Author(s):  
Erika C. Andrade ◽  
Veronica Musante ◽  
Atsuko Horiuchi ◽  
Hideo Matsuzaki ◽  
A. Harrison Brody ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Phosphatase 2A

scholarly journals Purification and Characterization of Protein Phosphatase 2A from Petals of the Tulip Tulipa gesnerina

BMB Reports ◽  
2006 ◽  
Vol 39 (6) ◽  
pp. 671-676 ◽  
Author(s):  
Md. Abul Kalam Azad ◽  
Yoshihiro Sawa ◽  
Takahiro Ishikawa ◽  
Hitoshi Shibata
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Purification And Characterization ◽  
Phosphatase 2A

scholarly journals AKT Regulates Mitotic Progression of Mammalian Cells by Phosphorylating MASTL, Leading to Protein Phosphatase 2A Inactivation

2020 ◽  
Vol 40 (10) ◽  
Author(s):  
Irfana Reshi ◽  
Misbah Un Nisa ◽  
Umer Farooq ◽  
Syed Qaaifah Gillani ◽  
Sameer Ahmed Bhat ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Mammalian Cells ◽  
Protein Phosphatase 2A ◽  
Critical Role ◽  
Mitotic Progression ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Mitotic Kinases ◽  
Colorectal Cell ◽  
Phosphatase 2A

ABSTRACT Microtubule-associated serine/threonine kinase like (MASTL), also known as Greatwall (Gwl) kinase, has an important role in the regulation of mitosis. By inhibiting protein phosphatase 2A (PP2A), it plays a crucial role in activating one of the most important mitotic kinases, known as cyclin-dependent kinase 1 (CDK1). MASTL has been seen to be upregulated in various types of cancers and is also involved in tumor recurrence. It is activated by CDK1 through phosphorylations in the activation/T-loop, but the complete mechanism of its activation is still unclear. Here, we report that AKT phosphorylates MASTL at residue T299, which plays a critical role in its activation. Our results suggest that AKT increases CDK1-mediated phosphorylation and hence the activity of MASTL, which, in turn, promotes mitotic progression through PP2A inhibition. We also show that the oncogenic potential of AKT is augmented by MASTL activation, since AKT-mediated proliferation in colorectal cell lines can be attenuated by inhibiting and/or silencing MASTL. In brief, we report that AKT plays an important role in the progression of mitosis in mammalian cells and that it does so through the phosphorylation and activation of MASTL.

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
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