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Article: Cloning of three novel neuronal Cdk5 activator binding proteins

TitleCloning of three novel neuronal Cdk5 activator binding proteins
Authors
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/gene
Citation
Gene, 2000, v. 242 n. 1-2, p. 285-294 How to Cite?
AbstractNeuronal Cdc2-like kinase (Nclk) is involved in the regulation of neuronal differentiation and neuro-cytoskeleton dynamics. The active kinase consists of a catalytic subunit, Cdk5, and a 25 kDa activator protein (p25(nck5a)) derived from a 35 kDa neuronal-specific protein (p35(nck5a)). As an extension of our previous study (Qi, Z., Tang, D., Zhu, X., Fujita, D.J., Wang, J.H., 1998. Association of neurofilament proteins with neuronal Cdk5 activator. J. Biol. Chem. 270, 2329-2335), which showed that neurofilament is one of the p35(nck5a)-associated proteins, we now report the isolation of three other novel p35(nck5a)-associated proteins using the yeast two-hybrid screen. The full-length forms of these three novel proteins, designated C42, C48 and C53, have a molecular mass of 66, 24, and 57 kDa, respectively. Northern analysis indicates that these novel proteins are widely expressed in human tissues, including the heart, brain, skeletal muscle, placenta, lung, liver, kidney and pancreas. The bacterially expressed glutathione S-transferase (GST)-fusion forms of these three proteins were able to co-precipitate p35(nck5a) complexed with Cdk5 from insect cell lysate. Among these three proteins, only C48 and C53 can be phosphorylated by Nclk, suggesting that they may be the substrates of Nclk. Sequence homology searches have suggested that the C48 protein is marginally related to restin protein, whereas the C42 protein has homologues of unknown function in Caenorhabditis elegans and Arabidopsis thaliana. (C) 2000 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149585
ISSN
2015 Impact Factor: 2.319
2015 SCImago Journal Rankings: 1.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChing, YPen_US
dc.contributor.authorQi, Zen_US
dc.contributor.authorWang, JHen_US
dc.date.accessioned2012-06-26T05:55:34Z-
dc.date.available2012-06-26T05:55:34Z-
dc.date.issued2000en_US
dc.identifier.citationGene, 2000, v. 242 n. 1-2, p. 285-294en_US
dc.identifier.issn0378-1119en_US
dc.identifier.urihttp://hdl.handle.net/10722/149585-
dc.description.abstractNeuronal Cdc2-like kinase (Nclk) is involved in the regulation of neuronal differentiation and neuro-cytoskeleton dynamics. The active kinase consists of a catalytic subunit, Cdk5, and a 25 kDa activator protein (p25(nck5a)) derived from a 35 kDa neuronal-specific protein (p35(nck5a)). As an extension of our previous study (Qi, Z., Tang, D., Zhu, X., Fujita, D.J., Wang, J.H., 1998. Association of neurofilament proteins with neuronal Cdk5 activator. J. Biol. Chem. 270, 2329-2335), which showed that neurofilament is one of the p35(nck5a)-associated proteins, we now report the isolation of three other novel p35(nck5a)-associated proteins using the yeast two-hybrid screen. The full-length forms of these three novel proteins, designated C42, C48 and C53, have a molecular mass of 66, 24, and 57 kDa, respectively. Northern analysis indicates that these novel proteins are widely expressed in human tissues, including the heart, brain, skeletal muscle, placenta, lung, liver, kidney and pancreas. The bacterially expressed glutathione S-transferase (GST)-fusion forms of these three proteins were able to co-precipitate p35(nck5a) complexed with Cdk5 from insect cell lysate. Among these three proteins, only C48 and C53 can be phosphorylated by Nclk, suggesting that they may be the substrates of Nclk. Sequence homology searches have suggested that the C48 protein is marginally related to restin protein, whereas the C42 protein has homologues of unknown function in Caenorhabditis elegans and Arabidopsis thaliana. (C) 2000 Elsevier Science 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/geneen_US
dc.relation.ispartofGeneen_US
dc.rightsGene. Copyright © Elsevier BV.-
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBlotting, Northernen_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshDna, Complementary - Chemistry - Geneticsen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshGlutathione Transferase - Genetics - Metabolismen_US
dc.subject.meshIntracellular Signaling Peptides And Proteinsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNerve Tissue Proteins - Genetics - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRecombinant Fusion Proteins - Genetics - Metabolismen_US
dc.subject.meshSequence Analysis, Dnaen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshTissue Distributionen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.titleCloning of three novel neuronal Cdk5 activator binding proteinsen_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/S0378-1119(99)00499-0en_US
dc.identifier.pmid10721722-
dc.identifier.scopuseid_2-s2.0-0033964878en_US
dc.identifier.hkuros53874-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033964878&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume242en_US
dc.identifier.issue1-2en_US
dc.identifier.spage285en_US
dc.identifier.epage294en_US
dc.identifier.isiWOS:000085278700031-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridChing, YP=7005431277en_US
dc.identifier.scopusauthoridQi, Z=7202289752en_US
dc.identifier.scopusauthoridWang, JH=7701314238en_US

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