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Article: Identification of a common protein association region in the neuronal Cdk5 activator

TitleIdentification of a common protein association region in the neuronal Cdk5 activator
Authors
Issue Date2000
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2000, v. 275 n. 41, p. 31763-31769 How to Cite?
AbstractCyclin-dependent protein kinase 5 (Cdk5) depends on the association with neuronal Cdk5 activator (Nck5a) for kinase activity. A variety of cellular proteins have been shown to undergo high affinity association with Nck5a, including three novel proteins, C42, C48, and C53 found by a yeast two-hybrid screen (Ching, Y. P., Qi, Z., and Wang, J. H. (2000) Gene 242, 285-294). The three proteins show competitive binding to Nck5a suggesting that they bind at a common site. The binding site has been mapped to a region of 26 amino acid residues (residues 145 to 170) at the N-terminal boundary of the kinase activation domain of Nck5a. This region of Nck5a contains an amphipathic α-helix whose hydrophobic face is involved in Cdk5 activation (Chin, K. T., Ohki, S, Tang, D., Cheng, H. C., Wang, J. H., and Zhang, M. (1999) J. Biol. Chem. 274, 7120-7127). Several lines of evidence suggest that Nck5a interacts with the binding proteins at the hydrophilic face of the amphipathic α-helix. First, the Nck5a-(145-170) peptide can bind Cdk5 and Nck5a-binding proteins simultaneously. Second, the association of Nck5a-145-170) to C48 can be markedly reduced by high ionic strength whereas the interaction between Nck5a and Cdk5 is not affected. Third, substitution of Glu157 by glutamine in Nck5a-(145-170) abolishes the peptide's ability to bind to the three Nck5a-binding proteins without diminishing its Cdk5 binding activity.
Persistent Identifierhttp://hdl.handle.net/10722/88000
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Xen_HK
dc.contributor.authorChing, YPen_HK
dc.contributor.authorLam, WHen_HK
dc.contributor.authorQi, Zen_HK
dc.contributor.authorZhang, Men_HK
dc.contributor.authorWang, JHen_HK
dc.date.accessioned2010-09-06T09:37:21Z-
dc.date.available2010-09-06T09:37:21Z-
dc.date.issued2000en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2000, v. 275 n. 41, p. 31763-31769en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/88000-
dc.description.abstractCyclin-dependent protein kinase 5 (Cdk5) depends on the association with neuronal Cdk5 activator (Nck5a) for kinase activity. A variety of cellular proteins have been shown to undergo high affinity association with Nck5a, including three novel proteins, C42, C48, and C53 found by a yeast two-hybrid screen (Ching, Y. P., Qi, Z., and Wang, J. H. (2000) Gene 242, 285-294). The three proteins show competitive binding to Nck5a suggesting that they bind at a common site. The binding site has been mapped to a region of 26 amino acid residues (residues 145 to 170) at the N-terminal boundary of the kinase activation domain of Nck5a. This region of Nck5a contains an amphipathic α-helix whose hydrophobic face is involved in Cdk5 activation (Chin, K. T., Ohki, S, Tang, D., Cheng, H. C., Wang, J. H., and Zhang, M. (1999) J. Biol. Chem. 274, 7120-7127). Several lines of evidence suggest that Nck5a interacts with the binding proteins at the hydrophilic face of the amphipathic α-helix. First, the Nck5a-(145-170) peptide can bind Cdk5 and Nck5a-binding proteins simultaneously. Second, the association of Nck5a-145-170) to C48 can be markedly reduced by high ionic strength whereas the interaction between Nck5a and Cdk5 is not affected. Third, substitution of Glu157 by glutamine in Nck5a-(145-170) abolishes the peptide's ability to bind to the three Nck5a-binding proteins without diminishing its Cdk5 binding activity.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshAmino Acid Substitution - geneticsen_HK
dc.subject.meshBinding, Competitiveen_HK
dc.subject.meshCarrier Proteins - metabolismen_HK
dc.subject.meshCyclin-Dependent Kinase 5en_HK
dc.subject.meshCyclin-Dependent Kinases - metabolismen_HK
dc.subject.meshEnzyme Activationen_HK
dc.subject.meshHumansen_HK
dc.subject.meshIntracellular Signaling Peptides and Proteinsen_HK
dc.subject.meshMacromolecular Substancesen_HK
dc.subject.meshMutation - geneticsen_HK
dc.subject.meshNerve Tissue Proteins - chemistry - genetics - metabolismen_HK
dc.subject.meshOsmolar Concentrationen_HK
dc.subject.meshPeptide Fragments - metabolismen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshRecombinant Fusion Proteins - metabolismen_HK
dc.titleIdentification of a common protein association region in the neuronal Cdk5 activatoren_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=275&issue=41&spage=31763&epage=9&date=2000&atitle=Identification+of+a+common+protein+association+region+in+the+neuronal+Cdk5+activatoren_HK
dc.identifier.emailChing, YP:ypching@hku.hken_HK
dc.identifier.authorityChing, YP=rp00469en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid10915792-
dc.identifier.scopuseid_2-s2.0-0034644730en_HK
dc.identifier.hkuros60029en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034644730&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume275en_HK
dc.identifier.issue41en_HK
dc.identifier.spage31763en_HK
dc.identifier.epage31769en_HK
dc.identifier.isiWOS:000089858900032-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWang, X=9333673900en_HK
dc.identifier.scopusauthoridChing, YP=7005431277en_HK
dc.identifier.scopusauthoridLam, WH=7203022052en_HK
dc.identifier.scopusauthoridQi, Z=7202289752en_HK
dc.identifier.scopusauthoridZhang, M=7601555100en_HK
dc.identifier.scopusauthoridWang, JH=7701314238en_HK

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