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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Reshi I,Nisa MU,Farooq U,Gillani SQ,Bhat SA,Sarwar Z,Nabi N,Fazili KM,Andrabi Sdoi
10.1128/MCB.00366-18subject
Has Abstractpub_date
2020-04-28 00:00:00issue
10eissn
0270-7306issn
1098-5549pii
MCB.00366-18journal_volume
40pub_type
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