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Non diaphanous formin delphilin acts as a barbed end capping protein

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dc.contributor.author DUTTA, PRIYANKA en_US
dc.contributor.author Das, Swagata en_US
dc.contributor.author Maitia, Sankar en_US
dc.date.accessioned 2019-07-01T05:31:29Z
dc.date.available 2019-07-01T05:31:29Z
dc.date.issued 2017-08 en_US
dc.identifier.citation Experimental Cell Research,357(2), 163-169. en_US
dc.identifier.issn 0014-4827 en_US
dc.identifier.issn 1090-2422 en_US
dc.identifier.uri http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3162
dc.identifier.uri https://doi.org/10.1016/j.yexcr.2017.05.014 en_US
dc.description.abstract Formins 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.iso en en_US
dc.publisher Elsevier B.V. en_US
dc.subject Formin Delphilin Expression en_US
dc.subject Actin and barbed end capping en_US
dc.subject FH2 domain of formins en_US
dc.subject Del-FH2 domain in vitro en_US
dc.subject 2017 en_US
dc.title Non diaphanous formin delphilin acts as a barbed end capping protein en_US
dc.type Article en_US
dc.contributor.department Dept. of Biology en_US
dc.identifier.sourcetitle Experimental Cell Research en_US
dc.publication.originofpublisher Foreign en_US


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