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Kinase-Independent Functions of MASTL in Cancer: A New Perspective on MASTL Targeting.

Authors
  • Conway, James Ronald William1
  • Närvä, Elisa1
  • Taskinen, Maria Emilia1
  • Ivaska, Johanna1, 2
  • 1 Turku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland. , (Finland)
  • 2 Department of Biochemistry, University of Turku, 20520 Turku, Finland. , (Finland)
Type
Published Article
Journal
Cells
Publisher
MDPI AG
Publication Date
Jul 06, 2020
Volume
9
Issue
7
Identifiers
DOI: 10.3390/cells9071624
PMID: 32640605
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Microtubule-associated serine/threonine kinase-like (MASTL; Greatwall) is a well-characterized kinase, whose catalytic role has been extensively studied in relation to cell-cycle acceleration. Importantly, MASTL has been implicated to play a substantial role in cancer progression and subsequent studies have shown that MASTL is a significant regulator of the cellular actomyosin cytoskeleton. Several kinases have non-catalytic properties, which are essential or even sufficient for their functions. Likewise, MASTL functions have been attributed both to kinase-dependent phosphorylation of downstream substrates, but also to kinase-independent regulation of the actomyosin contractile machinery. In this review, we aimed to highlight the catalytic and non-catalytic roles of MASTL in proliferation, migration, and invasion. Further, we discussed the implications of this dual role for therapeutic design.

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