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Article: Mechanistic studies of the mitotic activation of Mos

TitleMechanistic studies of the mitotic activation of Mos
Authors
Issue Date2006
Citation
Molecular And Cellular Biology, 2006, v. 26 n. 14, p. 5300-5309 How to Cite?
AbstractThe protein kinase Mos is responsible for the activation of MEK1 and p42 mitogen-activated protein kinase during Xenopus oocyte maturation and during mitosis in Xenopus egg extracts. Here we show that the activation of Mos depends upon the phosphorylation of Ser 3, a residue previously implicated in the regulation of Mos stability; the dephosphorylation of Ser 105, a previously unidentified phosphorylation site conserved in Mos proteins; and the regulated dissociation of Mos from CK2β. Mutation of Ser 3 to alanine and/or mutation of Ser 105 to glutamate produces a Mos protein that is defective for M-phase activation, as assessed by in vitro kinase assays, and defective for induction of oocyte maturation and maintenance of the spindle assembly checkpoint in extracts. Interestingly, Ser 105 is situated at the beginning of helix αC in the N-terminal lobe of the Mos kinase domain. Changes in the orientation of this helix have been previously implicated in the activation of Cdk2 and Src family tyrosine kinases. Our work suggests that Ser 105 dephosphorylation represents a novel mechanism for reorienting helix αC. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/171745
ISSN
2015 Impact Factor: 4.427
2015 SCImago Journal Rankings: 3.806
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYue, Jen_US
dc.contributor.authorFerrell Jr, JEen_US
dc.date.accessioned2012-10-30T06:16:45Z-
dc.date.available2012-10-30T06:16:45Z-
dc.date.issued2006en_US
dc.identifier.citationMolecular And Cellular Biology, 2006, v. 26 n. 14, p. 5300-5309en_US
dc.identifier.issn0270-7306en_US
dc.identifier.urihttp://hdl.handle.net/10722/171745-
dc.description.abstractThe protein kinase Mos is responsible for the activation of MEK1 and p42 mitogen-activated protein kinase during Xenopus oocyte maturation and during mitosis in Xenopus egg extracts. Here we show that the activation of Mos depends upon the phosphorylation of Ser 3, a residue previously implicated in the regulation of Mos stability; the dephosphorylation of Ser 105, a previously unidentified phosphorylation site conserved in Mos proteins; and the regulated dissociation of Mos from CK2β. Mutation of Ser 3 to alanine and/or mutation of Ser 105 to glutamate produces a Mos protein that is defective for M-phase activation, as assessed by in vitro kinase assays, and defective for induction of oocyte maturation and maintenance of the spindle assembly checkpoint in extracts. Interestingly, Ser 105 is situated at the beginning of helix αC in the N-terminal lobe of the Mos kinase domain. Changes in the orientation of this helix have been previously implicated in the activation of Cdk2 and Src family tyrosine kinases. Our work suggests that Ser 105 dephosphorylation represents a novel mechanism for reorienting helix αC. Copyright © 2006, American Society for Microbiology. All Rights Reserved.en_US
dc.languageengen_US
dc.relation.ispartofMolecular and Cellular Biologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCasein Kinase Ii - Metabolismen_US
dc.subject.meshCyclin B - Metabolismen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshFemaleen_US
dc.subject.meshMitosis - Physiologyen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshOocytes - Cytology - Enzymologyen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshProto-Oncogene Proteins C-Mos - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRecombinant Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshSerine - Chemistryen_US
dc.subject.meshXenopusen_US
dc.subject.meshXenopus Proteins - Chemistry - Genetics - Metabolismen_US
dc.titleMechanistic studies of the mitotic activation of Mosen_US
dc.typeArticleen_US
dc.identifier.emailYue, J:jyue@hku.hken_US
dc.identifier.authorityYue, J=rp00286en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/MCB.00273-06en_US
dc.identifier.pmid16809767-
dc.identifier.scopuseid_2-s2.0-33745806589en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33745806589&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume26en_US
dc.identifier.issue14en_US
dc.identifier.spage5300en_US
dc.identifier.epage5309en_US
dc.identifier.eissn1098-5549-
dc.identifier.isiWOS:000238918000009-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYue, J=7101875828en_US
dc.identifier.scopusauthoridFerrell Jr, JE=7005371587en_US

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