Proteomics

Dataset Information

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Identification of interactors of acetylated Ub


ABSTRACT: In this project we present the identification of interactors of mono-acetylated ubiquitin (Ub) variants from HEK293T whole cell extracts. Affinity enrichment coupled to high-resolution mass spectrometry followed by label-free quantification revealed the interactome of the respective mono-acetylated Ub variants.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Simon Kienle  

LAB HEAD: Prof. Dr. Martin Scheffner

PROVIDER: PXD028797 | Pride | 2022-10-14

REPOSITORIES: Pride

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Publications

Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function.

Kienle Simon Maria SM   Schneider Tobias T   Stuber Katrin K   Globisch Christoph C   Jansen Jasmin J   Stengel Florian F   Peter Christine C   Marx Andreas A   Kovermann Michael M   Scheffner Martin M  

Nature communications 20220916 1


Covalent attachment of ubiquitin (Ub) to proteins is a highly versatile posttranslational modification. Moreover, Ub is not only a modifier but itself is modified by phosphorylation and lysine acetylation. However, the functional consequences of Ub acetylation are poorly understood. By generation and comprehensive characterization of all seven possible mono-acetylated Ub variants, we show that each acetylation site has a particular impact on Ub structure. This is reflected in selective usage of  ...[more]

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