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Article: Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220

TitleInteraction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220
Authors
KeywordsHuman heart cDNA
Molecular adapter
Protein-protein interaction
Yeast two-hybrid system
Zinc finger protein
Issue Date2001
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, 2001, v. 84 n. 3, p. 556-566 How to Cite?
Abstract
Using a yeast two-hybrid library screen, we have identified that the heart specific FHL2 protein, fourand-a-half LIM protein 2, interacted with human DNA-binding nuclear protein, hNP220. Domain studies by the yeast two-hybrid interaction assay revealed that the second LIM domain together with the third and the fourth LIM domains of FHL2 were responsible to the binding with hNP220. Using green fluorescent protein (GFP)-FHL2 and blue fluorescent protein (BFP)-hNP220 fusion proteins co-expressed in the same cell, we demonstrated a direct interaction between FHL2 and hNP220 in individual nucleus by two-fusion Fluorescence Resonance Energy Transfer (FRET) assay. Besides, Western blot analysis using affinity-purified anti-FHL2 antipeptide antibodies confirmed a 32-kDa protein of FHL2 in heart only. Virtually no expression of FHL2 protein was detected in brain, liver, lung, kidney, testis, skeletal muscle, and spleen. Moreover, the expression of FHL2 protein was also detectable in the human diseased heart tissues. Our results imply that FHL2 protein can shuttle between cytoplasm and nucleus and may act as a molecular adapter to form a multicomplex with hNP220 in the nucleus, thus we speculate that FHL2 may be particularly important for heart muscle differentiation and the maintenance of the heart phenotype. © 2001 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/92329
ISSN
2013 Impact Factor: 3.368
ISI Accession Number ID
References

 

Author Affiliations
  1. Chinese University of Hong Kong
DC FieldValueLanguage
dc.contributor.authorNg, EKOen_HK
dc.contributor.authorChan, KKen_HK
dc.contributor.authorWong, CHen_HK
dc.contributor.authorTsui, SKWen_HK
dc.contributor.authorNgai, SMen_HK
dc.contributor.authorLee, SMYen_HK
dc.contributor.authorKotaka, Men_HK
dc.contributor.authorLee, CYen_HK
dc.contributor.authorWaye, MMYen_HK
dc.contributor.authorFung, KPen_HK
dc.date.accessioned2010-09-17T10:42:49Z-
dc.date.available2010-09-17T10:42:49Z-
dc.date.issued2001en_HK
dc.identifier.citationJournal Of Cellular Biochemistry, 2001, v. 84 n. 3, p. 556-566en_HK
dc.identifier.issn0730-2312en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92329-
dc.description.abstractUsing a yeast two-hybrid library screen, we have identified that the heart specific FHL2 protein, fourand-a-half LIM protein 2, interacted with human DNA-binding nuclear protein, hNP220. Domain studies by the yeast two-hybrid interaction assay revealed that the second LIM domain together with the third and the fourth LIM domains of FHL2 were responsible to the binding with hNP220. Using green fluorescent protein (GFP)-FHL2 and blue fluorescent protein (BFP)-hNP220 fusion proteins co-expressed in the same cell, we demonstrated a direct interaction between FHL2 and hNP220 in individual nucleus by two-fusion Fluorescence Resonance Energy Transfer (FRET) assay. Besides, Western blot analysis using affinity-purified anti-FHL2 antipeptide antibodies confirmed a 32-kDa protein of FHL2 in heart only. Virtually no expression of FHL2 protein was detected in brain, liver, lung, kidney, testis, skeletal muscle, and spleen. Moreover, the expression of FHL2 protein was also detectable in the human diseased heart tissues. Our results imply that FHL2 protein can shuttle between cytoplasm and nucleus and may act as a molecular adapter to form a multicomplex with hNP220 in the nucleus, thus we speculate that FHL2 may be particularly important for heart muscle differentiation and the maintenance of the heart phenotype. © 2001 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.subjectHuman heart cDNAen_HK
dc.subjectMolecular adapteren_HK
dc.subjectProtein-protein interactionen_HK
dc.subjectYeast two-hybrid systemen_HK
dc.subjectZinc finger proteinen_HK
dc.titleInteraction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220en_HK
dc.typeArticleen_HK
dc.identifier.emailNg, EKO: ngko@hku.hken_HK
dc.identifier.emailKotaka, M: masayo@hku.hken_HK
dc.identifier.authorityNg, EKO=rp01364en_HK
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/jcb.10041en_HK
dc.identifier.pmid11813260en_HK
dc.identifier.scopuseid_2-s2.0-18244364176en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-18244364176&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume84en_HK
dc.identifier.issue3en_HK
dc.identifier.spage556en_HK
dc.identifier.epage566en_HK
dc.identifier.isiWOS:000173358300012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridNg, EKO=21135553700en_HK
dc.identifier.scopusauthoridChan, KK=7406034649en_HK
dc.identifier.scopusauthoridWong, CH=8942307600en_HK
dc.identifier.scopusauthoridTsui, SKW=7004961364en_HK
dc.identifier.scopusauthoridNgai, SM=7006074219en_HK
dc.identifier.scopusauthoridLee, SMY=35233892600en_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.scopusauthoridLee, CY=7410142857en_HK
dc.identifier.scopusauthoridWaye, MMY=7006687733en_HK
dc.identifier.scopusauthoridFung, KP=35271657800en_HK

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