Mechanisms of Mitotic Kinase Regulation: A Structural Perspective

Protein kinases are major regulators of mitosis, with over 30% of the mitotic proteome phosphorylated on serines, threonines and tyrosines. The human genome encodes for 518 kinases that have a structurally conserved catalytic domain and includes about a dozen of cell division specific ones. Yet each...

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Published inFrontiers in cell and developmental biology Vol. 6; p. 6
Main Authors Welburn, Julie P I, Jeyaprakash, A Arockia
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 05.02.2018
Subjects
Cell and Developmental Biology
mechanism
mitosis
mitotic kinase
phosphorylation
structure
substrate
mechanism
mitosis
phosphorylation
structure
substrate
mitotic kinase
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Summary:Protein kinases are major regulators of mitosis, with over 30% of the mitotic proteome phosphorylated on serines, threonines and tyrosines. The human genome encodes for 518 kinases that have a structurally conserved catalytic domain and includes about a dozen of cell division specific ones. Yet each kinase has unique structural features that allow their distinct substrate recognition and modes of regulation. These unique regulatory features determine their accurate spatio-temporal activation critical for correct progression through mitosis and are exploited for therapeutic purposes. In this review, we will discuss the principles of mitotic kinase activation and the structural determinants that underlie functional specificity.
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Reviewed by: Darja Lavogina, University of Tartu, Estonia; Victor M. Bolanos-Garcia, Oxford Brookes University, United Kingdom
Edited by: Sabine Elowe, Laval University, Canada
This article was submitted to Cell Growth and Division, a section of the journal Frontiers in Cell and Developmental Biology
ISSN:2296-634X
2296-634X
DOI:10.3389/fcell.2018.00006