The functional diversity of Aurora kinases: a comprehensive review

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Abstract

Aurora kinases are serine/threonine kinases essential for the onset and progression of mitosis. Aurora members share a similar protein structure and kinase activity, but exhibit distinct cellular and subcellular localization. AurA favors the G2/M transition by promoting centrosome maturation and mitotic spindle assembly. AurB and AurC are chromosome-passenger complex proteins, crucial for chromosome binding to kinetochores and segregation of chromosomes. Cellular distribution of AurB is ubiquitous, while AurC expression is mainly restricted to meiotically-active germ cells. In human tumors, all Aurora kinase members play oncogenic roles related to their mitotic activity and promote cancer cell survival and proliferation. Furthermore, AurA plays tumor-promoting roles unrelated to mitosis, including tumor stemness, epithelial-to-mesenchymal transition and invasion. In this review, we aim to understand the functional interplay of Aurora kinases in various types of human cells, including tumor cells. The understanding of the functional diversity of Aurora kinases could help to evaluate their relevance as potential therapeutic targets in cancer.

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The protein kinase complement of the human genome.

G. Manning (2002)

We have catalogued the protein kinase complement of the human genome (the "kinome") using public and proprietary genomic, complementary DNA, and expressed sequence tag (EST) sequences. This provides a starting point for comprehensive analysis of protein phosphorylation in normal and disease states, as well as a detailed view of the current state of human genome analysis through a focus on one large gene family. We identify 518 putative protein kinase genes, of which 71 have not previously been reported or described as kinases, and we extend or correct the protein sequences of 56 more kinases. New genes include members of well-studied families as well as previously unidentified families, some of which are conserved in model organisms. Classification and comparison with model organism kinomes identified orthologous groups and highlighted expansions specific to human and other lineages. We also identified 106 protein kinase pseudogenes. Chromosomal mapping revealed several small clusters of kinase genes and revealed that 244 kinases map to disease loci or cancer amplicons.

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Protein kinases: evolution of dynamic regulatory proteins.

Susan S. Taylor, Alexandr Kornev (2011)

Eukayotic protein kinases evolved as a family of highly dynamic molecules with strictly organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for assembly of the entire molecule. Two non-consecutive hydrophobic structures termed "spines" anchor all the elements important for catalysis to the F-helix. They make firm, but flexible, connections within the molecule, providing a high level of internal dynamics of the protein kinase. During the course of evolution, protein kinases developed a universal regulatory mechanism associated with a large activation segment that can be dynamically folded and unfolded in the course of cell functioning. Protein kinases thus represent a unique, highly dynamic, and precisely regulated set of switches that control most biological events in eukaryotic cells. Copyright © 2010. Published by Elsevier Ltd.

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Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery.

Libor Macurek, Arne Lindqvist, Dan Lim … (2008)

Polo-like kinase-1 (PLK1) is an essential mitotic kinase regulating multiple aspects of the cell division process. Activation of PLK1 requires phosphorylation of a conserved threonine residue (Thr 210) in the T-loop of the PLK1 kinase domain, but the kinase responsible for this has not yet been affirmatively identified. Here we show that in human cells PLK1 activation occurs several hours before entry into mitosis, and requires aurora A (AURKA, also known as STK6)-dependent phosphorylation of Thr 210. We find that aurora A can directly phosphorylate PLK1 on Thr 210, and that activity of aurora A towards PLK1 is greatly enhanced by Bora (also known as C13orf34 and FLJ22624), a known cofactor for aurora A (ref. 7). We show that Bora/aurora-A-dependent phosphorylation is a prerequisite for PLK1 to promote mitotic entry after a checkpoint-dependent arrest. Importantly, expression of a PLK1-T210D phospho-mimicking mutant partially overcomes the requirement for aurora A in checkpoint recovery. Taken together, these data demonstrate that the initial activation of PLK1 is a primary function of aurora A.

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Author and article information

Contributors

Estelle Willems: estelle.willems@doct.uliege.be

Matthias Dedobbeleer: matthias.dedobbeleer@doct.uliege.be

Marina Digregorio: marina.digregorio@doct.uliege.be

Arnaud Lombard: arnaud.lombard@uliege.ac.be

Paul Noel Lumapat: paul.lumapat@gmail.com

Bernard Rogister: 32 4 366 59 50 , Bernard.Rogister@uliege.be

Journal

Journal ID (nlm-ta): Cell Div

Journal ID (iso-abbrev): Cell Div

Title: Cell Division

Publisher: BioMed Central (London )

ISSN (Electronic): 1747-1028

Publication date (Electronic): 19 September 2018

Publication date PMC-release: 19 September 2018

Publication date Collection: 2018

Volume: 13

Electronic Location Identifier: 7

Affiliations

[1 ]ISNI 0000 0001 0805 7253, GRID grid.4861.b, Laboratory of Nervous System Diseases and Therapy, GIGA-Neuroscience, , University of Liège, ; Avenue Hippocrate, 15, 4000 Liège, Belgium

[2 ]ISNI 0000 0000 8607 6858, GRID grid.411374.4, Department of Neurosurgery, , CHU of Liège, ; Liège, Belgium

[3 ]ISNI 0000 0000 8607 6858, GRID grid.411374.4, Department of Neurology, , CHU of Liège, ; Liège, Belgium

Article

Publisher ID: 40

DOI: 10.1186/s13008-018-0040-6

PMC ID: 6146527

PubMed ID: 30250494

SO-VID: e60743b3-18df-42de-b91b-2a5a4ba8c883

License:

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

History

Date received : 13 April 2018

Date accepted : 5 September 2018

Funding

Funded by: FundRef http://dx.doi.org/10.13039/501100002661, Fonds De La Recherche Scientifique - FNRS;

Funded by: FundRef http://dx.doi.org/10.13039/501100006673, Fonds Léon Fredericq;

Funded by: Erasmus Mundus Joint Doctorate in nanomedicine and pharmaceutical innovation (NANOFAR), European Erasmus Mundus

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ScienceOpen disciplines: Cell biology

Keywords: aurora kinase,mitosis,cancer

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ScienceOpen disciplines: Cell biology

Keywords: aurora kinase, mitosis, cancer

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The functional diversity of Aurora kinases: a comprehensive review

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Most cited references 139

The protein kinase complement of the human genome.

Protein kinases: evolution of dynamic regulatory proteins.

Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery.

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Cited by 118

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