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Publication Abstract from PubMed

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 A and hNpl4 at a resolution of 3.0 A. 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.

Structural basis for the interaction between human Npl4 and Npl4-binding motif of human Ufd1.,Nguyen TQ, My Le LT, Kim DH, Ko KS, Lee HT, Kim Nguyen YT, Kim HS, Han BW, Kang W, Yang JK Structure. 2022 Nov 3;30(11):1530-1537.e3. doi: 10.1016/j.str.2022.08.005. Epub , 2022 Sep 9. PMID:36087575^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.