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Article: Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220
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TitleInteraction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220
 
AuthorsNg, EKO1
Chan, KK1
Wong, CH1
Tsui, SKW1
Ngai, SM1
Lee, SMY1
Kotaka, M1
Lee, CY1
Waye, MMY1
Fung, KP1
 
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
 
CitationJournal Of Cellular Biochemistry, 2001, v. 84 n. 3, p. 556-566 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcb.10041
 
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.
 
ISSN0730-2312
2013 Impact Factor: 3.368
 
DOIhttp://dx.doi.org/10.1002/jcb.10041
 
ISI Accession Number IDWOS:000173358300012
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorNg, EKO
 
dc.contributor.authorChan, KK
 
dc.contributor.authorWong, CH
 
dc.contributor.authorTsui, SKW
 
dc.contributor.authorNgai, SM
 
dc.contributor.authorLee, SMY
 
dc.contributor.authorKotaka, M
 
dc.contributor.authorLee, CY
 
dc.contributor.authorWaye, MMY
 
dc.contributor.authorFung, KP
 
dc.date.accessioned2010-09-17T10:42:49Z
 
dc.date.available2010-09-17T10:42:49Z
 
dc.date.issued2001
 
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.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of Cellular Biochemistry, 2001, v. 84 n. 3, p. 556-566 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcb.10041
 
dc.identifier.doihttp://dx.doi.org/10.1002/jcb.10041
 
dc.identifier.epage566
 
dc.identifier.isiWOS:000173358300012
 
dc.identifier.issn0730-2312
2013 Impact Factor: 3.368
 
dc.identifier.issue3
 
dc.identifier.pmid11813260
 
dc.identifier.scopuseid_2-s2.0-18244364176
 
dc.identifier.spage556
 
dc.identifier.urihttp://hdl.handle.net/10722/92329
 
dc.identifier.volume84
 
dc.languageeng
 
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Cellular Biochemistry
 
dc.relation.referencesReferences in Scopus
 
dc.subjectHuman heart cDNA
 
dc.subjectMolecular adapter
 
dc.subjectProtein-protein interaction
 
dc.subjectYeast two-hybrid system
 
dc.subjectZinc finger protein
 
dc.titleInteraction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220
 
dc.typeArticle
 
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<contributor.author>Kotaka, M</contributor.author>
<contributor.author>Lee, CY</contributor.author>
<contributor.author>Waye, MMY</contributor.author>
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Author Affiliations
  1. Chinese University of Hong Kong