J Biol Chem: we found that the ubiquitin like protein Nedd8

On October 25, the Journal of biological chemistry published the research paper "Nedd8 ultimate buster-1 long (nub1l) protein promotions transfer of Nedd8 to protein for migration through the p97ufd1 / npl4 complex" by Hu Hongyu, research group, Institute of Biochemistry and cell, Shanghai Institute of Biological Sciences, Chinese Academy of Sciences This paper elucidates the molecular mechanism of the specific interaction of nub1l protein with Nedd8 and p97 to promote the degradation of Nedd8 by proteasome   Nedd8 is a ubiquitin like protein that can modify substrate protein It is known that Nedd8 regulates the activity of Cullin ring E3 ligase mainly by modifying Cullin protein, and then participates in the biological processes of cell cycle regulation, transcription and signal transduction Liu Shuai, a doctoral student, and other researchers used biochemical and molecular biological methods to discover that the asn51 residue of Nedd8 protein is necessary for the specific interaction between Nedd8 and nub1l Nub1l interacts with p97 through a VBM module, and the interaction is very important for nub1l to promote the degradation of Nedd8 P97, assisted by its cofactors ufd1 and npl4, is directly involved in the degradation of Nedd8 in proteasome P97ufd1 / npl4 can form a stable complex with nub1l, while its binding with Nedd8 depends on the presence of ATP In addition, nub1l and p97 can reduce the level of Nedd8 of cullin-1 protein This further proves that NUB1L and P97 control the level of protein NEDD8 modification by promoting the degradation of NEDD8 by proteasome These studies revealed the molecular mechanism of nub1l promoting the degradation of Nedd8 through p97ufd1 / npl4, which is of great significance for people to understand the regulatory mechanism of Nedd8 modification   The research was supported by funds from the Ministry of science and technology, the State Foundation Committee and the Chinese Academy of Sciences.