Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

Yusuke Sato; Hikaru Tsuchiya; Atsushi Yamagata; Kei Okatsu; Keiji Tanaka; Yasushi Saeki; Shuya Fukai

doi:10.1038/s41467-019-13697-y

Nature Communications (Dec 2019)

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4

Yusuke Sato,
Hikaru Tsuchiya,
Atsushi Yamagata,
Kei Okatsu,
Keiji Tanaka,
Yasushi Saeki,
Shuya Fukai

Affiliations

Yusuke Sato: Institute for Quantitative Biosciences, The University of Tokyo
Hikaru Tsuchiya: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Atsushi Yamagata: Institute for Quantitative Biosciences, The University of Tokyo
Kei Okatsu: Institute for Quantitative Biosciences, The University of Tokyo
Keiji Tanaka: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Yasushi Saeki: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Shuya Fukai: Institute for Quantitative Biosciences, The University of Tokyo

DOI: https://doi.org/10.1038/s41467-019-13697-y
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 13

Abstract

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The Lys48-linked polyubiquitin-mediated proteasomal degradation in yeast depends on Cdc48 and its cofactors Ufd1 and Npl4. Here, the authors present crystal structures of Npl4 bound to Lys48-linked diubiquitin and the Npl4-binding motif of Ufd1, providing insights into the reaction mechanism of the Cdc48- Ufd1/Npl4 complex.

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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