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dc.contributor.authorJensen, Mikkel Herholdt
dc.contributor.authorMorris, Eliza J.
dc.contributor.authorHuang, Renjian
dc.contributor.authorRebowski, Grzegorz
dc.contributor.authorDominguez, Roberto
dc.contributor.authorWeitz, David A.
dc.contributor.authorMoore, Jeffrey R.
dc.contributor.authorWang, Chih-Lueh Albert
dc.date.accessioned2019-10-09T13:56:34Z
dc.date.issued2012
dc.identifier.citationJensen, Mikkel Herholdt, Eliza J. Morris, Renjian Huang, Grzegorz Rebowski, Roberto Dominguez, David A. Weitz, Jeffrey R. Moore, and Chih-Lueh Albert Wang. 2012. “The Conformational State of Actin Filaments Regulates Branching by Actin-Related Protein 2/3 (Arp2/3) Complex.” Journal of Biological Chemistry287 (37): 31447–53. https://doi.org/10.1074/jbc.M112.350421.
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41511258*
dc.description.abstractActin is a highly ubiquitous protein in eukaryotic cells that plays a crucial role in cell mechanics and motility. Cell motility is driven by assembling actin as polymerizing actin drives cell protrusions in a process closely involving a host of other actin-binding proteins, notably the actin-related protein 2/3 (Arp2/3) complex, which nucleates actin and forms branched filamentous structures. The Arp2/3 complex preferentially binds specific actin networks at the cell leading edge and forms branched filamentous structures, which drive cell protrusions, but the exact regulatory mechanism behind this process is not well understood. Here we show using in vitro imaging and binding assays that a fragment of the actin-binding protein caldesmon added to polymerizing actin increases the Arp2/3-mediated branching activity, whereas it has no effect on branch formation when binding to aged actin filaments. Because this caldesmon effect is shown to be independent of nucleotide hydrolysis and phosphate release from actin, our results suggest a mechanism by which caldesmon maintains newly polymerized actin in a distinct state that has a higher affinity for the Arp2/3 complex. Our data show that this new state does not affect the level of cooperativity of binding by Arp2/3 complex or its distribution on actin. This presents a novel regulatory mechanism by which caldesmon, and potentially other actin-binding proteins, regulates the interactions of actin with its binding partners.
dc.language.isoen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dash.licenseLAA
dc.titleThe Conformational State of Actin Filaments Regulates Branching by Actin-related Protein 2/3 (Arp2/3) Complex
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalThe Journal of Biological Chemistry
dash.depositing.authorWeitz, David A.::4c144b06be6d094b21dbe2dd12dbef76::600
dc.date.available2019-10-09T13:56:34Z
dash.workflow.comments1Science Serial ID 109801
dc.identifier.doi10.1074/jbc.M112.350421
dash.source.volume287;37
dash.source.page31447


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