Ub-ProT reveals global length and composition of protein ubiquitylation in cells

Hikaru Tsuchiya; Daocharad Burana; Fumiaki Ohtake; Naoko Arai; Ai Kaiho; Masayuki Komada; Keiji Tanaka; Yasushi Saeki

doi:10.1038/s41467-018-02869-x

Nature Communications (Feb 2018)

Ub-ProT reveals global length and composition of protein ubiquitylation in cells

Hikaru Tsuchiya,
Daocharad Burana,
Fumiaki Ohtake,
Naoko Arai,
Ai Kaiho,
Masayuki Komada,
Keiji Tanaka,
Yasushi Saeki

Affiliations

Hikaru Tsuchiya: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Daocharad Burana: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Fumiaki Ohtake: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Naoko Arai: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Ai Kaiho: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Masayuki Komada: Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology
Keiji Tanaka: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Yasushi Saeki: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science

DOI: https://doi.org/10.1038/s41467-018-02869-x
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 10

Abstract

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Ubiquitylation is a dynamic post-translational modification involved in the regulation of numerous cellular processes. Here the authors describe Ub-ProT: a method to measure the length of substrate-attached ubiquitin chains in biological samples, and demonstrate a critical role for chain length in directing substrates to specific cellular pathways.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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