Identification of a Tissue-Restricted Isoform of SIRT1 Defines a Regulatory Domain that Encodes Specificity.

Abstract:

:The conserved NAD+-dependent deacylase SIRT1 plays pivotal, sometimes contrasting, roles in diverse physiological and pathophysiological conditions. In this study, we uncover a tissue-restricted isoform of SIRT1 (SIRT1-ΔE2) that lacks exon 2 (E2). Candidate-based screening of SIRT1 substrates demonstrated that the domain encoded by this exon plays a key role in specifying SIRT1 protein-protein interactions. The E2 domain of SIRT1 was both necessary and sufficient for PGC1α binding, enhanced interaction with p53, and thus downstream functions. Since SIRT1-FL and SIRT1-ΔE2 were found to have similar intrinsic catalytic activities, we propose that the E2 domain tethers specific substrate proteins. Given the absence of SIRT1-ΔE2 in liver, our findings provide insight into the role of the E2 domain in specifying "metabolic functions" of SIRT1-FL. Identification of SIRT1-ΔE2 and the conserved specificity domain will enhance our understanding of SIRT1 and guide the development of therapeutic interventions.

journal_name

Cell Rep

journal_title

Cell reports

authors

Deota S,Chattopadhyay T,Ramachandran D,Armstrong E,Camacho B,Maniyadath B,Fulzele A,Gonzalez-de-Peredo A,Denu JM,Kolthur-Seetharam U

doi

10.1016/j.celrep.2017.03.012

subject

Has Abstract

pub_date

2017-03-28 00:00:00

pages

3069-3077

issue

13

issn

2211-1247

pii

S2211-1247(17)30329-7

journal_volume

18

pub_type

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