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Article: Interaction of hCLIM1, an enigma family protein, with α-actinin 2

TitleInteraction of hCLIM1, an enigma family protein, with α-actinin 2
Authors
Keywordsα-actinin 2
LIM domain
PDZ domain
Yeast two-hybrid screening
Issue Date2000
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
Citation
Journal Of Cellular Biochemistry, 2000, v. 78 n. 4, p. 558-565 How to Cite?
AbstractEnigma proteins are proteins that possess a PDZ domain at the amino terminal and one to three LIM domains at the carboxyl terminal. They are cytoplasmic proteins that are involved with the cytoskeleton and signal transduction pathway. By virtue of the two protein interacting domains, they are capable of protein-protein interactions. Here we report a study on a human Enigma protein hclim1, in particular. Our study describes the interaction of the human 36kda carboxyl terminal Llm domain protein (hclim1), the human homologue of CLP36 in rat, with α-actinin 2, the skeletal muscle isoform of α-actinin, hclim1 protein was shown to interact with α-actinin 2 by yeast two-hybrid screening and immunochemical analyses. Yeast two-hybrid analyses also demonstrated that the LIM domain of hclim1 binds to the EF-hand region of α-actinin 2, defining a new mode of LIM domain interactions. Immunofluorescent study demonstrates that hCLIM1 colocalizes with α-actinin at the Z-disks in human myocardium. Taken together, our experimental results suggest that hCLIM1 is a novel cytoskeletal protein and may act as an adapter that brings other proteins to the cytoskeleton. (C) 2000 Wiley-liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/92225
ISSN
2015 Impact Factor: 3.446
2015 SCImago Journal Rankings: 1.520
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKotaka, Men_HK
dc.contributor.authorKostin, Sen_HK
dc.contributor.authorNgai, SMen_HK
dc.contributor.authorChan, KKen_HK
dc.contributor.authorLau, YMen_HK
dc.contributor.authorLee, SMYen_HK
dc.contributor.authorLi, HYen_HK
dc.contributor.authorNg, EKOen_HK
dc.contributor.authorSchaper, Jen_HK
dc.contributor.authorTsui, SKWen_HK
dc.contributor.authorFung, KPen_HK
dc.contributor.authorLee, CYen_HK
dc.contributor.authorWaye, MMYen_HK
dc.date.accessioned2010-09-17T10:39:46Z-
dc.date.available2010-09-17T10:39:46Z-
dc.date.issued2000en_HK
dc.identifier.citationJournal Of Cellular Biochemistry, 2000, v. 78 n. 4, p. 558-565en_HK
dc.identifier.issn0730-2312en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92225-
dc.description.abstractEnigma proteins are proteins that possess a PDZ domain at the amino terminal and one to three LIM domains at the carboxyl terminal. They are cytoplasmic proteins that are involved with the cytoskeleton and signal transduction pathway. By virtue of the two protein interacting domains, they are capable of protein-protein interactions. Here we report a study on a human Enigma protein hclim1, in particular. Our study describes the interaction of the human 36kda carboxyl terminal Llm domain protein (hclim1), the human homologue of CLP36 in rat, with α-actinin 2, the skeletal muscle isoform of α-actinin, hclim1 protein was shown to interact with α-actinin 2 by yeast two-hybrid screening and immunochemical analyses. Yeast two-hybrid analyses also demonstrated that the LIM domain of hclim1 binds to the EF-hand region of α-actinin 2, defining a new mode of LIM domain interactions. Immunofluorescent study demonstrates that hCLIM1 colocalizes with α-actinin at the Z-disks in human myocardium. Taken together, our experimental results suggest that hCLIM1 is a novel cytoskeletal protein and may act as an adapter that brings other proteins to the cytoskeleton. (C) 2000 Wiley-liss, Inc.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503en_HK
dc.relation.ispartofJournal of Cellular Biochemistryen_HK
dc.subjectα-actinin 2en_HK
dc.subjectLIM domainen_HK
dc.subjectPDZ domainen_HK
dc.subjectYeast two-hybrid screeningen_HK
dc.titleInteraction of hCLIM1, an enigma family protein, with α-actinin 2en_HK
dc.typeArticleen_HK
dc.identifier.emailKotaka, M: masayo@hku.hken_HK
dc.identifier.emailNg, EKO: ngko@hku.hken_HK
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.identifier.authorityNg, EKO=rp01364en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-Ien_HK
dc.identifier.pmid10861853en_HK
dc.identifier.scopuseid_2-s2.0-0033897296en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033897296&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume78en_HK
dc.identifier.issue4en_HK
dc.identifier.spage558en_HK
dc.identifier.epage565en_HK
dc.identifier.isiWOS:000088462100005-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.scopusauthoridKostin, S=7003379106en_HK
dc.identifier.scopusauthoridNgai, SM=7006074219en_HK
dc.identifier.scopusauthoridChan, KK=7406034649en_HK
dc.identifier.scopusauthoridLau, YM=14420993500en_HK
dc.identifier.scopusauthoridLee, SMY=35233892600en_HK
dc.identifier.scopusauthoridLi, HY=12762326800en_HK
dc.identifier.scopusauthoridNg, EKO=21135553700en_HK
dc.identifier.scopusauthoridSchaper, J=7102151442en_HK
dc.identifier.scopusauthoridTsui, SKW=7004961364en_HK
dc.identifier.scopusauthoridFung, KP=35271657800en_HK
dc.identifier.scopusauthoridLee, CY=7410142857en_HK
dc.identifier.scopusauthoridWaye, MMY=7006687733en_HK

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