File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Nek2A kinase regulates the localization of numatrin to centrosome in mitosis

TitleNek2A kinase regulates the localization of numatrin to centrosome in mitosis
Authors
KeywordsCentromere
Centrosome
DAPI, 4,6-diamidino-2-phenylindole
Mitotic spindle
Nek2A
NIMA, never in mitosis A
Numatrin
SDS-PAGE, SDS-poly-acrylamide gel electrophoresis
Issue Date2004
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2004, v. 575 n. 1-3, p. 112-118 How to Cite?
AbstractChromosome segregation in mitosis is orchestrated by the kinetochore and spindle microtubules stemming from two centrosomes. Our recent studies demonstrated the importance of Nek2A in faithful chromosome segregation during mitosis. Here, we report that Nek2A regulates the function of numatrin in mitosis. The biochemical interaction between Nek2A and numatrin in mitotic cells was revealed by a set of reciprocal immunoprecipitation experiments using Nek2A and numatrin antibodies, respectively. The interaction is validated by a pull-down assay using recombinant Nek2A and numatrin proteins. Moreover, our immunofluorescence studies demonstrate that numatrin becomes centrosome-associated as the cell enters into mitosis and depart from the centrosome after sister chromatid separation in anaphase. The co-localization of numatrin and Nek2A to the centrosome suggests their interaction with and involvement in centrosome function. Indeed, elimination of Nek2A kinase by siRNA diminished its association with the centrosome. Furthermore, we show that numatrin is phosphorylated by wild type but not kinase-death Nek2A. Our studies suggest that the Nek2A kinase cascade is essential for the localization of numatrin to the centrosome. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/136784
ISSN
2023 Impact Factor: 3.0
2023 SCImago Journal Rankings: 1.208
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYao, Jen_HK
dc.contributor.authorFu, Cen_HK
dc.contributor.authorDing, Xen_HK
dc.contributor.authorGuo, Zen_HK
dc.contributor.authorZenreski, Aen_HK
dc.contributor.authorChen, Yen_HK
dc.contributor.authorAhmed, Ken_HK
dc.contributor.authorLiao, Jen_HK
dc.contributor.authorDou, Zen_HK
dc.contributor.authorYao, Xen_HK
dc.date.accessioned2011-07-29T02:12:11Z-
dc.date.available2011-07-29T02:12:11Z-
dc.date.issued2004en_HK
dc.identifier.citationFebs Letters, 2004, v. 575 n. 1-3, p. 112-118en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/136784-
dc.description.abstractChromosome segregation in mitosis is orchestrated by the kinetochore and spindle microtubules stemming from two centrosomes. Our recent studies demonstrated the importance of Nek2A in faithful chromosome segregation during mitosis. Here, we report that Nek2A regulates the function of numatrin in mitosis. The biochemical interaction between Nek2A and numatrin in mitotic cells was revealed by a set of reciprocal immunoprecipitation experiments using Nek2A and numatrin antibodies, respectively. The interaction is validated by a pull-down assay using recombinant Nek2A and numatrin proteins. Moreover, our immunofluorescence studies demonstrate that numatrin becomes centrosome-associated as the cell enters into mitosis and depart from the centrosome after sister chromatid separation in anaphase. The co-localization of numatrin and Nek2A to the centrosome suggests their interaction with and involvement in centrosome function. Indeed, elimination of Nek2A kinase by siRNA diminished its association with the centrosome. Furthermore, we show that numatrin is phosphorylated by wild type but not kinase-death Nek2A. Our studies suggest that the Nek2A kinase cascade is essential for the localization of numatrin to the centrosome. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.subjectCentromere-
dc.subjectCentrosome-
dc.subjectDAPI, 4,6-diamidino-2-phenylindole-
dc.subjectMitotic spindle-
dc.subjectNek2A-
dc.subjectNIMA, never in mitosis A-
dc.subjectNumatrin-
dc.subjectSDS-PAGE, SDS-poly-acrylamide gel electrophoresis-
dc.subject.meshCentrosome - metabolismen_HK
dc.subject.meshHeLa Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshImmunohistochemistryen_HK
dc.subject.meshMitosis - physiologyen_HK
dc.subject.meshNuclear Proteins - metabolismen_HK
dc.subject.meshProtein-Serine-Threonine Kinases - genetics - metabolismen_HK
dc.subject.meshRNA, Small Interfering - genetics - metabolismen_HK
dc.subject.meshRecombinant Fusion Proteins - genetics - metabolismen_HK
dc.titleNek2A kinase regulates the localization of numatrin to centrosome in mitosisen_HK
dc.typeArticleen_HK
dc.identifier.emailFu, C:chuanhai@hku.hken_HK
dc.identifier.authorityFu, C=rp01515en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.febslet.2004.08.047en_HK
dc.identifier.pmid15388344-
dc.identifier.scopuseid_2-s2.0-4544283606en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-4544283606&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume575en_HK
dc.identifier.issue1-3en_HK
dc.identifier.spage112en_HK
dc.identifier.epage118en_HK
dc.identifier.isiWOS:000224286900021-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridYao, J=7403503922en_HK
dc.identifier.scopusauthoridFu, C=8583808400en_HK
dc.identifier.scopusauthoridDing, X=12140021800en_HK
dc.identifier.scopusauthoridGuo, Z=7404658143en_HK
dc.identifier.scopusauthoridZenreski, A=6505532487en_HK
dc.identifier.scopusauthoridChen, Y=7601443903en_HK
dc.identifier.scopusauthoridAhmed, K=7202086800en_HK
dc.identifier.scopusauthoridLiao, J=37117419600en_HK
dc.identifier.scopusauthoridDou, Z=7007006881en_HK
dc.identifier.scopusauthoridYao, X=7402530401en_HK
dc.identifier.issnl0014-5793-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats