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Article: α-Chimaerin exists in a functional complex with the Cdk5 kinase in brain

Titleα-Chimaerin exists in a functional complex with the Cdk5 kinase in brain
Authors
Qi, RZChing, YPKung, HFWang, JH
KeywordsCdk, cyclin-dependent kinase
Cdk5
Cdk5 activator
Chimaerin
DTT, dithiothreitol
GSH, glutathione
GST, glutathione S-transferase
PBS, phosphate-buffered saline
Protein-protein interaction
Issue Date2004
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2004, v. 561 n. 1-3, p. 177-180 How to Cite?
DOI: http://dx.doi.org/10.1016/S0014-5793(04)00174-7
AbstractCyclin-dependent kinase 5 (Cdk5) in association with its neuronal activators p35 and p39 shows a complex involvement in the control of neurocytoskeletal dynamics. Here we show that α-chimaerin, a GTPase-activating protein specific for Rac and Cdc42, is a p35-binding protein. The interaction domains of p35 and α-chimaerin were delineated. In transfected HeLa cells, p35 and α-chimaerin displayed an overlapping distribution pattern and they could be co-immunoprecipitated from the cell lysate. As α-chimaerin has a regulatory function in actin repolymerization, these results suggested that the regulation of neurocytoskeleton dynamics by Cdk5 is mediated at least in part via α-chimaerin. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149629
ISSN
0014-5793
2023 Impact Factor: 3.0
2023 SCImago Journal Rankings: 1.208
ISI Accession Number ID
WOS:000220244100031
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorQi, RZen_US
dc.contributor.authorChing, YPen_US
dc.contributor.authorKung, HFen_US
dc.contributor.authorWang, JHen_US
dc.date.accessioned2012-06-26T05:56:15Z-
dc.date.available2012-06-26T05:56:15Z-
dc.date.issued2004en_US
dc.identifier.citationFebs Letters, 2004, v. 561 n. 1-3, p. 177-180en_US
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/10722/149629-
dc.description.abstractCyclin-dependent kinase 5 (Cdk5) in association with its neuronal activators p35 and p39 shows a complex involvement in the control of neurocytoskeletal dynamics. Here we show that α-chimaerin, a GTPase-activating protein specific for Rac and Cdc42, is a p35-binding protein. The interaction domains of p35 and α-chimaerin were delineated. In transfected HeLa cells, p35 and α-chimaerin displayed an overlapping distribution pattern and they could be co-immunoprecipitated from the cell lysate. As α-chimaerin has a regulatory function in actin repolymerization, these results suggested that the regulation of neurocytoskeleton dynamics by Cdk5 is mediated at least in part via α-chimaerin. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_US
dc.relation.ispartofFEBS Lettersen_US
dc.subjectCdk, cyclin-dependent kinase-
dc.subjectCdk5-
dc.subjectCdk5 activator-
dc.subjectChimaerin-
dc.subjectDTT, dithiothreitol-
dc.subjectGSH, glutathione-
dc.subjectGST, glutathione S-transferase-
dc.subjectPBS, phosphate-buffered saline-
dc.subjectProtein-protein interaction-
dc.subject.meshBrain - Enzymologyen_US
dc.subject.meshChimerin 1 - Analysis - Genetics - Metabolismen_US
dc.subject.meshCyclin-Dependent Kinase 5en_US
dc.subject.meshCyclin-Dependent Kinases - Analysis - Genetics - Metabolismen_US
dc.subject.meshCytoskeleton - Metabolismen_US
dc.subject.meshGene Libraryen_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHumansen_US
dc.subject.meshNeuronsen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshTransfectionen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.titleα-Chimaerin exists in a functional complex with the Cdk5 kinase in brainen_US
dc.typeArticleen_US
dc.identifier.emailChing, YP:ypching@hku.hken_US
dc.identifier.authorityChing, YP=rp00469en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0014-5793(04)00174-7en_US
dc.identifier.pmid15013773-
dc.identifier.scopuseid_2-s2.0-1542358137en_US
dc.identifier.hkuros87542-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1542358137&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume561en_US
dc.identifier.issue1-3en_US
dc.identifier.spage177en_US
dc.identifier.epage180en_US
dc.identifier.isiWOS:000220244100031-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridQi, RZ=7006273649en_US
dc.identifier.scopusauthoridChing, YP=7005431277en_US
dc.identifier.scopusauthoridKung, HF=7402514190en_US
dc.identifier.scopusauthoridWang, JH=7701314238en_US
dc.identifier.citeulike1699532-
dc.identifier.issnl0014-5793-

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