Kim, Kyung Hee Ha, Byung Hak Kim, Eunice EunKyeong 2024-01-19T23:33:58Z 2024-01-19T23:33:58Z 2021-09-03 2018-01 0014-5793 https://pubs.kist.re.kr/handle/201004/121852 Ubiquitin and ubiquitin-like proteins (Ubls) are involved in a variety of cellular functions, and dysfunction of these proteins often leads to disease, thus requiring the precise molecular recognition of the partner. Here, we report a structural basis for the recognition of Ufm1 by the Ufm1-specific protease (UfSP), both from Caenorhabditis elegans. Ufm1 functions in endoplasmic reticulum homeostasis, cell cycle regulation, and dysfunctions of this protein can result in breast cancer and neurological disorders. The structure reveals that in addition to the extended-structure at the C-terminus of cUfm1, the interactions made by the completely conserved residues in Ufm1 orthologs, Pro88-Val92, corresponding to P6-P2 positions from the cleavage site, seem to be important for the specific recognition of Ufm1 by cUfSP. English WILEY UBIQUITIN-LIKE PROTEINS PROTEASES ENZYME PATHWAYS SUITE NMR UBIQUITIN-FOLD-MODIFIER-1 AUTOPHAGY INSIGHTS REVEALS Structural basis for Ufm1 recognition by UfSP Article 10.1002/1873-3468.12951 1 FEBS LETTERS, v.592, no.2, pp.263 - 273 FEBS LETTERS 592 2 263 273 scie scopus 000423684200012 2-s2.0-85040038994 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article UBIQUITIN-LIKE PROTEINS PROTEASES ENZYME PATHWAYS SUITE NMR UBIQUITIN-FOLD-MODIFIER-1 AUTOPHAGY INSIGHTS REVEALS complex crystal structure molecular recognition ubiquitin-fold modifier 1 Ufm1-specific protease