Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3162
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dc.contributor.authorDUTTA, PRIYANKAen_US
dc.contributor.authorDas, Swagataen_US
dc.contributor.authorMaitia, Sankaren_US
dc.date.accessioned2019-07-01T05:31:29Z-
dc.date.available2019-07-01T05:31:29Z-
dc.date.issued2017-08en_US
dc.identifier.citationExperimental Cell Research,357(2), 163-169.en_US
dc.identifier.issn0014-4827en_US
dc.identifier.issn1090-2422en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3162-
dc.identifier.urihttps://doi.org/10.1016/j.yexcr.2017.05.014en_US
dc.description.abstractFormins are multi domain proteins present ubiquitously in all eukaryotes from lower fungi to higher vertebrates. Formins are characterized by the presence of formin homology domain-2 (FH2) and formin homology domain-1 (FH1). There are fifteen different formins present in mouse and human. Among these metazoan formins, Delphilin is a unique formin having two PDZ domains at the N-terminus and FH1, FH2 domain at the C-terminus respectively. In this study we observed that Delphilin binds to actin filaments, and Delphilin inhibits actin filament elongation like barbed end capping protein CapZ. In vitro, Delphilin stabilized actin filaments by inhibiting actin filament depolymerisation. Therefore, our study demonstrates Delphilin as an actin-filament capping protein.en_US
dc.language.isoenen_US
dc.publisherElsevier B.V.en_US
dc.subjectFormin Delphilin Expressionen_US
dc.subjectActin and barbed end cappingen_US
dc.subjectFH2 domain of forminsen_US
dc.subjectDel-FH2 domain in vitroen_US
dc.subject2017en_US
dc.titleNon diaphanous formin delphilin acts as a barbed end capping proteinen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Biologyen_US
dc.identifier.sourcetitleExperimental Cell Researchen_US
dc.publication.originofpublisherForeignen_US
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