Mechanisms of Mitotic Kinase Regulation: A Structural Perspective

Julie P I Welburn, Jeyaprakash Arulanandam

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original languageEnglish
Pages (from-to)6
JournalFrontiers in Cell and Developmental Biology
Volume6
DOIs
Publication statusPublished - 5 Feb 2018

Keywords

  • Mitotic kinase
  • mitosis
  • phosphorylation
  • structure
  • mechanism
  • substrate

Access to Document

  • fcell-06-00006

    © 2018 Welburn and Jeyaprakash. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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