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Acetylation of SUMO 2 at lysine 11 favors the formation of non‐canonical SUMO chains
Author(s) -
Gärtner Anne,
Wagner Kristina,
Hölper Soraya,
Kunz Kathrin,
Rodriguez Manuel S,
Müller Stefan
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201846117
Subject(s) - sumo protein , acetylation , sumo enzymes , lysine , ubiquitin ligase , ubiquitin , microbiology and biotechnology , biology , dna ligase , biochemistry , chemistry , amino acid , gene
Post‐translational modifications by ubiquitin‐related SUMO modifiers regulate cellular signaling networks and protein homeostasis. While SUMO 1 is mainly conjugated to proteins as a monomer, SUMO 2/3 can form polymeric chains. Poly‐ SUMO ylation is best understood in the SUMO ‐targeted ubiquitin ligase (StUbL) pathway, where chains prime proteins for subsequent ubiquitylation by StUbLs. SUMO chains typically form in response to genotoxic or proteotoxic stress and are preferentially linked via lysine 11 of SUMO 2/3. Here, we report that K11 of SUMO 2/3 undergoes reversible acetylation with SIRT 1 being the K11 deacetylase. In a purified in vitro system, acetylation of SUMO 2/3 impairs chain formation and restricts chain length. In a cellular context, however, K11 acetyl‐mimicking SUMO 2 does not affect the StUbL pathway, indicating that in cells non‐canonical chains are more prevalent. MS ‐based SUMO proteomics indeed identified non‐canonical chain types under basal and stress conditions. Importantly, mimicking K11 acetylation alters chain architecture by favoring K5‐ and K35‐linked chains, while inhibiting K7 and K21 linkages. These data provide insight into SUMO chain signaling and point to a role of K11 acetylation as a modulator of SUMO 2/3 chains.