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Sci. Signal., 7 January 2014
Vol. 7, Issue 307, p. pc1
[DOI: 10.1126/scisignal.2004994]


Science Signaling Podcast: 7 January 2014

Michaela U. Gack1,2 and Annalisa M. VanHook3

1 Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.
2 Microbiology Division, New England Primate Research Center, Harvard Medical School, 1 Pine Hill Drive, Southborough, MA 01772, USA.
3 Web Editor, Science Signaling, American Association for the Advancement of Science, 1200 New York Avenue, NW, Washington, DC 20005, USA.

Abstract: This Podcast features an interview with Michaela Gack, author of a Research Article that appears in the 7 January 2014 issue of Science Signaling, about a posttranslational modification that affects the response to viral infection. Ubiquitination is a reversible posttranslational modification that controls the stability, activity, or localization of proteins. There are several chemically distinct types of ubiquitination, and target proteins may be ubiquitinated on multiple sites. Where and how ubiquitin is attached to a substrate can have profoundly different effects on that substrate, so the regulation of protein function by ubiquitination is complex and dynamic. Pauli et al. report that the ubiquitin-specific protease USP15 promotes interferon production to prolong the antiviral response by stabilizing the ubiquitin E3 ligase TRIM25.

Citation: M. U. Gack, A. M. VanHook, Science Signaling Podcast: 7 January 2014. Sci. Signal. 7, pc1 (2014).

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