Structural basis for the interaction between human Npl4 and Npl4-binding motif of human Ufd1
- Authors
- Nguyen, T.Q.; My, Le L.T.; Kim, D.H.; Ko, K.S.; Lee, H.T.; Kim, Nguyen Y.T.; Kim, H.S.; Han, B.W.; Kang, Wonchull; Yang, Jin Kuk
- Issue Date
- Nov-2022
- Publisher
- Cell Press
- Keywords
- endoplasmic reticulum-associated degradation, ERAD; Npl4; p97; ubiquitin; Ufd1
- Citation
- Structure, v.30, no.11, pp.1530 - 1537.e3
- Journal Title
- Structure
- Volume
- 30
- Number
- 11
- Start Page
- 1530
- End Page
- 1537.e3
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/43193
- DOI
- 10.1016/j.str.2022.08.005
- ISSN
- 0969-2126
- Abstract
- The heterodimer of human ubiquitin fusion degradation 1 (hUfd1) and human nuclear protein localization 4 (hNpl4) is a major cofactor of human p97 adenosine triphosphatase (ATPase). The p97-Ufd1-Npl4 complex translocates the ubiquitin-conjugated proteins from the endoplasmic reticulum membrane to the cytoplasm. Ubiquitinated proteins are then degraded by the proteasome. The structures of Npl4 and Ufd1-Npl4 (UN) complex in Saccharomyces cerevisiae have been recently reported; however, the structures of hNpl4 and the human UN complex remain unknown. Here, we report the crystal structures of the human UN complex at a resolution of 2.7 Å and hNpl4 at a resolution of 3.0 Å. We also present atomic details and characterization of the human UN complex. Crystallographic studies and site-directed mutagenesis of the hUfd1 residues involved in the interaction with hNpl4 revealed the atomic details of the two proteins. © 2022 Elsevier Ltd
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