Article: Differential subcellular localization and activity of kelch repeat proteins KLHDC1 and KLHDC2.

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TitleDifferential subcellular localization and activity of kelch repeat proteins KLHDC1 and KLHDC2.
AuthorsChin, KT1
Xu, HT1
Ching, YP1
Jin, DY1
Issue Date2007
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0300-8177
CitationMolecular And Cellular Biochemistry, 2007, v. 296 n. 1-2, p. 109-119 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s11010-006-9304-6
AbstractWe have previously identified and characterized human KLHDC2/HCLP-1, a kelch repeat protein that interacts with and inhibits transcription factor LZIP. In this study, we identified and characterized a paralog of KLHDC2 called KLHDC1. KLHDC1 and KLHDC2 share about 50% identity at the level of amino acid sequence and both gene loci localize to human chromosome 14q21.3. This cluster of KLHDC1 and KLHDC2 genes is highly conserved in vertebrates ranging from pufferfish to human. Both genes are expressed highly in skeletal muscle, but weakly in various other tissues. While KLHDC2 was predominantly found in the nucleus, KLHDC1 is a cytoplasmic protein. Neither KLHDC1 nor KLHDC2 binds to actin. In addition, KLHDC1 was unable to inhibit LZIP/CREB3-mediated transcriptional activation. Thus, KLHDC1 and KLHDC2 have differential localization and activity in cultured mammalian cells.
ISSN0300-8177
2011 Impact Factor: 2.057
2011 SCImago Journal Rankings: 0.195
DOIhttp://dx.doi.org/10.1007/s11010-006-9304-6
DC Field
Value
dc.contributor.authorChin, KT
dc.contributor.authorXu, HT
dc.contributor.authorChing, YP
dc.contributor.authorJin, DY
dc.date.accessioned2009-04-03T07:40:42Z
dc.date.available2009-04-03T07:40:42Z
dc.date.issued2007
dc.description.abstractWe have previously identified and characterized human KLHDC2/HCLP-1, a kelch repeat protein that interacts with and inhibits transcription factor LZIP. In this study, we identified and characterized a paralog of KLHDC2 called KLHDC1. KLHDC1 and KLHDC2 share about 50% identity at the level of amino acid sequence and both gene loci localize to human chromosome 14q21.3. This cluster of KLHDC1 and KLHDC2 genes is highly conserved in vertebrates ranging from pufferfish to human. Both genes are expressed highly in skeletal muscle, but weakly in various other tissues. While KLHDC2 was predominantly found in the nucleus, KLHDC1 is a cytoplasmic protein. Neither KLHDC1 nor KLHDC2 binds to actin. In addition, KLHDC1 was unable to inhibit LZIP/CREB3-mediated transcriptional activation. Thus, KLHDC1 and KLHDC2 have differential localization and activity in cultured mammalian cells.
dc.description.naturepostprint
dc.identifier.citationMolecular And Cellular Biochemistry, 2007, v. 296 n. 1-2, p. 109-119 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s11010-006-9304-6
dc.identifier.citeulike1196787
dc.identifier.doihttp://dx.doi.org/10.1007/s11010-006-9304-6
dc.identifier.epage119
dc.identifier.hkuros126753
dc.identifier.isiWOS:000244691900013
dc.identifier.issn0300-8177
2011 Impact Factor: 2.057
2011 SCImago Journal Rankings: 0.195
dc.identifier.issue1-2
dc.identifier.pmid16964437
dc.identifier.scopuseid_2-s2.0-34447542890
dc.identifier.spage109
dc.identifier.urihttp://hdl.handle.net/10722/54237
dc.identifier.volume296
dc.languageeng
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0300-8177
dc.publisher.placeUnited States
dc.relation.ispartofMolecular and cellular biochemistry
dc.rightsThe original publication is available at www.springerlink.com
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
dc.subject.meshAntibiotics, Antineoplastic - metabolism
dc.subject.meshAntigens, Neoplasm - classification - genetics - metabolism
dc.subject.meshCarrier Proteins - genetics - metabolism
dc.subject.meshSequence Homology, Amino Acid
dc.subject.meshTissue Distribution
dc.titleDifferential subcellular localization and activity of kelch repeat proteins KLHDC1 and KLHDC2.
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong