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Article: Translocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization

TitleTranslocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization
Authors
Issue Date2001
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0886-1544/
Citation
Cell Motility And The Cytoskeleton, 2001, v. 48 n. 1, p. 11-23 How to Cite?
AbstractLIM domain proteins are found to be important regulators in cell growth, cell fate determination, cell differentiation, and remodeling of the cell cytoskeleton. Human Four-and-a-half LIM-only protein 2 (FHL2) is expressed predominantly in human heart and is only slightly expressed in skeletal muscle. Since FHL2 is an abundant protein in human heart, it may play an important role in the regulation of cell differentiation and myofibrillogenesis of heart at defined subcellular compartment. Therefore, we hypothesized that FHL2 act as a multi-functional protein by the specific arrangement of the LIM domains of FHL2 and that one of the LIM domains of FHL2 can function as an anchor and localizes it into a specific subcellular compartment in a cell type specific manner to regulate myofibrillogenesis. From our reuslts, we observed that FHL2 is localized at the focal adhesions of the C2C12, H9C2 myoblast as well as a nonmyogenic cell line, HepG2 cells. Colocalization of vinculin-CFP and FHL2-GFP at focal adhesions was also observed in cell lines. Site-directed mutagenesis, in turn, suggested that the second LIM domain-LIM2 is essential for its specific localization to focal adhesions. Moreover, FHL2 was observed along with F-actin and focal adhesion of C2C12 and H9C2 myotubes. Finally, we believe that FHL2 moves from focal adhesions and then stays at the Z-discs of terminally differentiated heart muscle. © 2001 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/171695
ISSN
2011 Impact Factor: 4.194
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, HYen_US
dc.contributor.authorKotaka, Men_US
dc.contributor.authorKostin, Sen_US
dc.contributor.authorLee, SMYen_US
dc.contributor.authorKok, LDSen_US
dc.contributor.authorChan, KKen_US
dc.contributor.authorTsui, SKWen_US
dc.contributor.authorSchaper, Jen_US
dc.contributor.authorZimmermann, Ren_US
dc.contributor.authorLee, CYen_US
dc.contributor.authorFung, KPen_US
dc.contributor.authorWaye, MMYen_US
dc.date.accessioned2012-10-30T06:16:25Z-
dc.date.available2012-10-30T06:16:25Z-
dc.date.issued2001en_US
dc.identifier.citationCell Motility And The Cytoskeleton, 2001, v. 48 n. 1, p. 11-23en_US
dc.identifier.issn0886-1544en_US
dc.identifier.urihttp://hdl.handle.net/10722/171695-
dc.description.abstractLIM domain proteins are found to be important regulators in cell growth, cell fate determination, cell differentiation, and remodeling of the cell cytoskeleton. Human Four-and-a-half LIM-only protein 2 (FHL2) is expressed predominantly in human heart and is only slightly expressed in skeletal muscle. Since FHL2 is an abundant protein in human heart, it may play an important role in the regulation of cell differentiation and myofibrillogenesis of heart at defined subcellular compartment. Therefore, we hypothesized that FHL2 act as a multi-functional protein by the specific arrangement of the LIM domains of FHL2 and that one of the LIM domains of FHL2 can function as an anchor and localizes it into a specific subcellular compartment in a cell type specific manner to regulate myofibrillogenesis. From our reuslts, we observed that FHL2 is localized at the focal adhesions of the C2C12, H9C2 myoblast as well as a nonmyogenic cell line, HepG2 cells. Colocalization of vinculin-CFP and FHL2-GFP at focal adhesions was also observed in cell lines. Site-directed mutagenesis, in turn, suggested that the second LIM domain-LIM2 is essential for its specific localization to focal adhesions. Moreover, FHL2 was observed along with F-actin and focal adhesion of C2C12 and H9C2 myotubes. Finally, we believe that FHL2 moves from focal adhesions and then stays at the Z-discs of terminally differentiated heart muscle. © 2001 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0886-1544/en_US
dc.relation.ispartofCell Motility and the Cytoskeletonen_US
dc.subject.meshActins - Metabolismen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshCell Differentiationen_US
dc.subject.meshCell Lineen_US
dc.subject.meshEye Proteins - Metabolismen_US
dc.subject.meshFocal Adhesions - Metabolism - Ultrastructureen_US
dc.subject.meshGreen Fluorescent Proteinsen_US
dc.subject.meshHomeodomain Proteins - Chemistry - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshLim-Homeodomain Proteinsen_US
dc.subject.meshLuminescent Proteins - Metabolismen_US
dc.subject.meshMembrane Proteins - Metabolismen_US
dc.subject.meshMicroscopy, Confocalen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMuscle Proteinsen_US
dc.subject.meshMuscles - Cytology - Metabolism - Ultrastructureen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshMyocardium - Metabolism - Ultrastructureen_US
dc.subject.meshMyofibrils - Metabolismen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshSequence Alignmenten_US
dc.subject.meshTranscription Factorsen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.subject.meshVinculin - Metabolismen_US
dc.titleTranslocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localizationen_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/1097-0169(200101)48:1<11::AID-CM2>3.0.CO;2-Ien_US
dc.identifier.pmid11124707-
dc.identifier.scopuseid_2-s2.0-0035173456en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035173456&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume48en_US
dc.identifier.issue1en_US
dc.identifier.spage11en_US
dc.identifier.epage23en_US
dc.identifier.isiWOS:000166073500002-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLi, HY=12762326800en_US
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridKostin, S=7003379106en_US
dc.identifier.scopusauthoridLee, SMY=35233892600en_US
dc.identifier.scopusauthoridKok, LDS=7005396433en_US
dc.identifier.scopusauthoridChan, KK=7406034649en_US
dc.identifier.scopusauthoridTsui, SKW=7004961364en_US
dc.identifier.scopusauthoridSchaper, J=7102151442en_US
dc.identifier.scopusauthoridZimmermann, R=23108110300en_US
dc.identifier.scopusauthoridLee, CY=7410142857en_US
dc.identifier.scopusauthoridFung, KP=7202934739en_US
dc.identifier.scopusauthoridWaye, MMY=7006687733en_US

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