Mechanisms of Mitotic Kinase Regulation: A Structural Perspective

Julie P I Welburn; Jeyaprakash Arulanandam

doi:10.3389/fcell.2018.00006

Mechanisms of Mitotic Kinase Regulation: A Structural Perspective

Julie P I Welburn, Jeyaprakash Arulanandam

School of Biological Sciences

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 language	English
Pages (from-to)	6
Journal	Frontiers in Cell and Developmental Biology
Volume	6
DOIs	https://doi.org/10.3389/fcell.2018.00006
Publication status	Published - 5 Feb 2018

Keywords / Materials (for Non-textual outputs)

Mitotic kinase
mitosis
phosphorylation
structure
mechanism
substrate

Access to Document

10.3389/fcell.2018.00006

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.
Final published version, 1.53 MBLicence: Creative Commons: Attribution (CC-BY)

Molecular Mechanisms of Centromere Inheritance and Kinetochore Function
Arulanandam, J. (Principal Investigator)
UK-based charities
4/01/17 → 4/10/22
Project: Research
Wellcome Centre for Cell Biology
Tollervey, D. (Principal Investigator)
UK-based charities
1/12/16 → 1/12/21
Project: Research
Single molecule studies of microtubule motor complexes
Welburn, J. (Principal Investigator)
Other (Learned Society)
1/10/16 → 30/09/17
Project: Research

Cite this

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title = "Mechanisms of Mitotic Kinase Regulation: A Structural Perspective",

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.",

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author = "Welburn, {Julie P I} and Jeyaprakash Arulanandam",

year = "2018",

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T2 - A Structural Perspective

AU - Welburn, Julie P I

AU - Arulanandam, Jeyaprakash

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N2 - 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.

AB - 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.

KW - Mitotic kinase

KW - mitosis

KW - phosphorylation

KW - structure

KW - mechanism

KW - substrate

U2 - 10.3389/fcell.2018.00006

DO - 10.3389/fcell.2018.00006

M3 - Article

C2 - 29459892

SN - 2296-634X

VL - 6

SP - 6

JO - Frontiers in Cell and Developmental Biology

JF - Frontiers in Cell and Developmental Biology

ER -

Mechanisms of Mitotic Kinase Regulation: A Structural Perspective

Abstract

Keywords / Materials (for Non-textual outputs)

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Projects

Molecular Mechanisms of Centromere Inheritance and Kinetochore Function

Wellcome Centre for Cell Biology

Single molecule studies of microtubule motor complexes

Cite this