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Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform. | LitMetric

Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform.

J Mol Biol

Department of Molecular Biology, University of Bergen, Postbox 7803, 5020 Bergen, Norway. Electronic address:

Published: April 2014

AI Article Synopsis

Article Abstract

Sirtuin-2 (SIRT2), the cytoplasmic member of the sirtuin family, has been implicated in the deacetylation of nuclear proteins. Although the enzyme has been reported to be located to the nucleus during G2/M phase, its spectrum of targets suggests functions in the nucleus throughout the cell cycle. While a nucleocytoplasmic shuttling mechanism has been proposed for SIRT2, recent studies have indicated the presence of a constitutively nuclear isoform. Here we report the identification of a novel splice variant (isoform 5) of SIRT2 that lacks a nuclear export signal and encodes a predominantly nuclear isoform. This novel isoform 5 fails to show deacetylase activity using several assays, both in vitro and in vivo, and we are led to conclude that this isoform is catalytically inactive. Nevertheless, it retains the ability to interact with p300, a known interaction partner. Moreover, changes in intrinsic tryptophan fluorescence upon denaturation indicate that the protein is properly folded. These data, together with computational analyses, confirm the structural integrity of the catalytic domain. Our results suggest an activity-independent nuclear function of the novel isoform.

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Source
http://dx.doi.org/10.1016/j.jmb.2013.10.027DOI Listing

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