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Sci. Signal., 14 June 2011
Vol. 4, Issue 177, p. pc11
[DOI: 10.1126/scisignal.2002240]

PODCASTS

Science Signaling Podcast: 14 June 2011

Richard Treisman1, Neil Q. McDonald2,3,4, Stéphane Mouilleron2, and Annalisa M. VanHook5

1 Transcription Group, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.
2 Structural Biology Group, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.
3 Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
4 Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
5 Web Editor, Science Signaling, American Association for the Advancement of Science, 1200 New York Avenue, N.W., Washington, DC 20005, USA.

Abstract: This podcast features a conversation with Richard Treisman, Neil McDonald, and Stéphane Mouilleron, authors of a Research Article published in the 14 June 2011 issue of Science Signaling. The authors discuss how increasing concentrations of monomeric actin trap the transcriptional coactivator MRTF-A, which couples changes in actin concentration to gene expression, in the cytoplasm, thus preventing it from activating expression of target genes. The crystal structure of actin bound to MRTF-A reveals an unusual mode of actin binding to a target protein.

Citation: R. Treisman, N. Q. McDonald, S. Mouilleron, A. M. VanHook, Science Signaling Podcast: 14 June 2011. Sci. Signal. 4, pc11 (2011).

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Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882