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Article: Identification of an Autoinhibitory Domain of p21-activated Protein Kinase 5

TitleIdentification of an Autoinhibitory Domain of p21-activated Protein Kinase 5
Authors
KeywordsBiology
Biochemistry
Issue Date2003
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, 2003, v. 278 n. 36, p. 33621-33624 How to Cite?
AbstractThe p21-activated protein kinases (Paks) are serine/threonine protein kinases activated by binding to Rho family small GTPases, Rac and Cdc42. Recently, Pak family members have been subdivided into two groups, I and II. Group II Paks, including Pak4, Pak5, and Pak6, does not contain the highly conserved autoinhibitory domain that is found in the group I Paks members, i.e. Pak1, Pak2, and Pak3. In the present study, we have purified the glutathione S-transferase fusion form of Pak5 and shown for the first time that Pak5 autophosphorylation can be activated by GTP bound form of Cdc42. Mutation of histidine residues 19 and 22 to leucine on the p21-binding domain of Pak5 completely abolished the binding of Cdc42 and the Cdc42-mediated autophosphorylation. On the other hand, mutation of tyrosine 40 to cysteine of Cdc42 did not knockout the binding of Pak5. Analysis of C-terminal deletion mutants has identified an autoinhibitory fragment of Pak5 that is absent from other group II Pak family members. Taken together, these results suggest that Pak5, like Pak1, contains an autoinhibitory domain and its activity is regulated by Cdc42.
Persistent Identifierhttp://hdl.handle.net/10722/48655
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChing, YPen_HK
dc.contributor.authorLeong, VYLen_HK
dc.contributor.authorWong, CMen_HK
dc.contributor.authorKung, HFen_HK
dc.date.accessioned2008-05-22T04:20:22Z-
dc.date.available2008-05-22T04:20:22Z-
dc.date.issued2003en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2003, v. 278 n. 36, p. 33621-33624en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48655-
dc.description.abstractThe p21-activated protein kinases (Paks) are serine/threonine protein kinases activated by binding to Rho family small GTPases, Rac and Cdc42. Recently, Pak family members have been subdivided into two groups, I and II. Group II Paks, including Pak4, Pak5, and Pak6, does not contain the highly conserved autoinhibitory domain that is found in the group I Paks members, i.e. Pak1, Pak2, and Pak3. In the present study, we have purified the glutathione S-transferase fusion form of Pak5 and shown for the first time that Pak5 autophosphorylation can be activated by GTP bound form of Cdc42. Mutation of histidine residues 19 and 22 to leucine on the p21-binding domain of Pak5 completely abolished the binding of Cdc42 and the Cdc42-mediated autophosphorylation. On the other hand, mutation of tyrosine 40 to cysteine of Cdc42 did not knockout the binding of Pak5. Analysis of C-terminal deletion mutants has identified an autoinhibitory fragment of Pak5 that is absent from other group II Pak family members. Taken together, these results suggest that Pak5, like Pak1, contains an autoinhibitory domain and its activity is regulated by Cdc42.en_HK
dc.format.extent828045 bytes-
dc.format.extent1797545 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
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.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectBiologyen_HK
dc.subjectBiochemistryen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshCell Lineen_HK
dc.subject.meshGene Deletionen_HK
dc.subject.meshGlutathione Transferase - metabolismen_HK
dc.subject.meshGuanosine Triphosphate - metabolismen_HK
dc.subject.meshHistidine - chemistryen_HK
dc.subject.meshHumansen_HK
dc.subject.meshLeucine - chemistryen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshMutationen_HK
dc.subject.meshPhosphorylationen_HK
dc.subject.meshPlasmids - metabolismen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshProtein-Serine-Threonine Kinases - metabolismen_HK
dc.subject.meshRecombinant Fusion Proteins - metabolismen_HK
dc.subject.meshSequence Homology, Amino Aciden_HK
dc.subject.meshTransfectionen_HK
dc.subject.meshTyrosine - chemistryen_HK
dc.subject.meshcdc42 GTP-Binding Protein - metabolismen_HK
dc.subject.meshp21-Activated Kinasesen_HK
dc.titleIdentification of an Autoinhibitory Domain of p21-activated Protein Kinase 5en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=278&issue=36&spage=33621&epage=33624&date=2003&atitle=Identification+of+an+autoinhibitory+domain+of+p21-activated+protein+kinase+5en_HK
dc.identifier.emailChing, YP:ypching@hku.hken_HK
dc.identifier.emailWong, CM:wispwong@hkucc.hku.hken_HK
dc.identifier.authorityChing, YP=rp00469en_HK
dc.identifier.authorityWong, CM=rp01489en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1074/jbc.C300234200en_HK
dc.identifier.pmid12860998-
dc.identifier.scopuseid_2-s2.0-0141817910en_HK
dc.identifier.hkuros87286-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0141817910&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume278en_HK
dc.identifier.issue36en_HK
dc.identifier.spage33621en_HK
dc.identifier.epage33624en_HK
dc.identifier.isiWOS:000185047500004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChing, YP=7005431277en_HK
dc.identifier.scopusauthoridLeong, VYL=36832636400en_HK
dc.identifier.scopusauthoridWong, CM=18134632400en_HK
dc.identifier.scopusauthoridKung, HF=7402514190en_HK

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