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Article: How protein kinases co-ordinate mitosis in animal cells

TitleHow protein kinases co-ordinate mitosis in animal cells
Authors
KeywordsKinase
Phosphatase
Cell cycle
Mitosis
Phosphorylation
Issue Date2011
Citation
Biochemical Journal, 2011, v. 435, n. 1, p. 17-31 How to Cite?
AbstractMitosis is associated with profound changes in cell physiology and a spectacular surge in protein phosphorylation. To accomplish these, a remarkably large portion of the kinome is involved in the process. In the present review, we will focus on classic mitotic kinases, such as cyclin-dependent kinases, Polo-like kinases and Aurora kinases, as well as more recently characterized players such as NIMA (never in mitosis in Aspergillus nidulans)-related kinases, Greatwall and Haspin. Together, these kinases co-ordinate the proper timing and fidelity of processes including centrosomal functions, spindle assembly and microtubule-kinetochore attachment, as well as sister chromatid separation and cytokinesis. A recurrent theme of the mitotic kinase network is the prevalence of elaborated feedback loops that ensure bistable conditions. Sequential phosphorylation and priming phosphorylation on substrates are also frequently employed. Another important concept is the role of scaffolds, such as centrosomes for protein kinases during mitosis. Elucidating the entire repertoire of mitotic kinases, their functions, regulation and interactions is critical for our understanding of normal cell growth and in diseases such as cancers. ©The Authors Journal compilation ©2011 Biochemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/307106
ISSN
2023 Impact Factor: 4.4
2023 SCImago Journal Rankings: 1.612
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMa, Hoi Tang-
dc.contributor.authorPoon, Randy Y.C.-
dc.date.accessioned2021-11-03T06:21:57Z-
dc.date.available2021-11-03T06:21:57Z-
dc.date.issued2011-
dc.identifier.citationBiochemical Journal, 2011, v. 435, n. 1, p. 17-31-
dc.identifier.issn0264-6021-
dc.identifier.urihttp://hdl.handle.net/10722/307106-
dc.description.abstractMitosis is associated with profound changes in cell physiology and a spectacular surge in protein phosphorylation. To accomplish these, a remarkably large portion of the kinome is involved in the process. In the present review, we will focus on classic mitotic kinases, such as cyclin-dependent kinases, Polo-like kinases and Aurora kinases, as well as more recently characterized players such as NIMA (never in mitosis in Aspergillus nidulans)-related kinases, Greatwall and Haspin. Together, these kinases co-ordinate the proper timing and fidelity of processes including centrosomal functions, spindle assembly and microtubule-kinetochore attachment, as well as sister chromatid separation and cytokinesis. A recurrent theme of the mitotic kinase network is the prevalence of elaborated feedback loops that ensure bistable conditions. Sequential phosphorylation and priming phosphorylation on substrates are also frequently employed. Another important concept is the role of scaffolds, such as centrosomes for protein kinases during mitosis. Elucidating the entire repertoire of mitotic kinases, their functions, regulation and interactions is critical for our understanding of normal cell growth and in diseases such as cancers. ©The Authors Journal compilation ©2011 Biochemical Society.-
dc.languageeng-
dc.relation.ispartofBiochemical Journal-
dc.subjectKinase-
dc.subjectPhosphatase-
dc.subjectCell cycle-
dc.subjectMitosis-
dc.subjectPhosphorylation-
dc.titleHow protein kinases co-ordinate mitosis in animal cells-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1042/BJ20100284-
dc.identifier.pmid21406064-
dc.identifier.scopuseid_2-s2.0-79952832468-
dc.identifier.volume435-
dc.identifier.issue1-
dc.identifier.spage17-
dc.identifier.epage31-
dc.identifier.eissn1470-8728-
dc.identifier.isiWOS:000289182100002-

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