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- Publisher Website: 10.1042/BJ20100284
- Scopus: eid_2-s2.0-79952832468
- PMID: 21406064
- WOS: WOS:000289182100002
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Article: How protein kinases co-ordinate mitosis in animal cells
Title | How protein kinases co-ordinate mitosis in animal cells |
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Authors | |
Keywords | Kinase Phosphatase Cell cycle Mitosis Phosphorylation |
Issue Date | 2011 |
Citation | Biochemical Journal, 2011, v. 435, n. 1, p. 17-31 How to Cite? |
Abstract | Mitosis 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 Identifier | http://hdl.handle.net/10722/307106 |
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 1.612 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Ma, Hoi Tang | - |
dc.contributor.author | Poon, Randy Y.C. | - |
dc.date.accessioned | 2021-11-03T06:21:57Z | - |
dc.date.available | 2021-11-03T06:21:57Z | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | Biochemical Journal, 2011, v. 435, n. 1, p. 17-31 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://hdl.handle.net/10722/307106 | - |
dc.description.abstract | Mitosis 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.language | eng | - |
dc.relation.ispartof | Biochemical Journal | - |
dc.subject | Kinase | - |
dc.subject | Phosphatase | - |
dc.subject | Cell cycle | - |
dc.subject | Mitosis | - |
dc.subject | Phosphorylation | - |
dc.title | How protein kinases co-ordinate mitosis in animal cells | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1042/BJ20100284 | - |
dc.identifier.pmid | 21406064 | - |
dc.identifier.scopus | eid_2-s2.0-79952832468 | - |
dc.identifier.volume | 435 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 17 | - |
dc.identifier.epage | 31 | - |
dc.identifier.eissn | 1470-8728 | - |
dc.identifier.isi | WOS:000289182100002 | - |