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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Main Authors: Julie P. I. Welburn, A. Arockia Jeyaprakash
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-02-01
Series:Frontiers in Cell and Developmental Biology
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fcell.2018.00006/full
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author Julie P. I. Welburn
A. Arockia Jeyaprakash
author_facet Julie P. I. Welburn
A. Arockia Jeyaprakash
author_sort Julie P. I. Welburn
collection DOAJ
description 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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spelling doaj.art-9d2336d823114ff0aed99f419f88cbb62022-12-21T17:57:54ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2018-02-01610.3389/fcell.2018.00006326532Mechanisms of Mitotic Kinase Regulation: A Structural PerspectiveJulie P. I. WelburnA. Arockia JeyaprakashProtein 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.http://journal.frontiersin.org/article/10.3389/fcell.2018.00006/fullmitotic kinasemitosisphosphorylationstructuremechanismsubstrate
spellingShingle Julie P. I. Welburn
A. Arockia Jeyaprakash
Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
Frontiers in Cell and Developmental Biology
mitotic kinase
mitosis
phosphorylation
structure
mechanism
substrate
title Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
title_full Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
title_fullStr Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
title_full_unstemmed Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
title_short Mechanisms of Mitotic Kinase Regulation: A Structural Perspective
title_sort mechanisms of mitotic kinase regulation a structural perspective
topic mitotic kinase
mitosis
phosphorylation
structure
mechanism
substrate
url http://journal.frontiersin.org/article/10.3389/fcell.2018.00006/full
work_keys_str_mv AT juliepiwelburn mechanismsofmitotickinaseregulationastructuralperspective
AT aarockiajeyaprakash mechanismsofmitotickinaseregulationastructuralperspective