Ha, Byung Hak Jeon, Young Joo Shin, Sang Chul Tatsumi, Kanako Komatsu, Masaaki Tanaka, Keiji Watson, Christopher M. Wallis, Gillian Chung, Chin Ha Kim, Eunice EunKyeong 2024-01-20T17:30:45Z 2024-01-20T17:30:45Z 2021-09-02 2011-03-25 0021-9258 https://pubs.kist.re.kr/handle/201004/130509 Ubiquitin- fold modifier 1 (Ufm1)-specific protease 2 (UfSP2) is a cysteine protease that is responsible for the release of Ufm1 from Ufm1-conjugated cellular proteins, as well as for the generation of mature Ufm1 from its precursor. The 2.6A resolution crystal structure of mouse UfSP2 reveals that it is composed of two domains. The C-terminal catalytic domain is similar to UfSP1 with Cys294, Asp418, His420, Tyr282, and a regulatory loop participating in catalysis. The novel N-terminal domain shows a unique structure and plays a role in the recognition of its cellular substrate C20orf116 and thus in the recruitment of UfSP2 to the endoplasmic reticulum, where C20orf116 predominantly localizes. Mutagenesis studies were carried out to provide the structural basis for understanding the loss of catalytic activity observed in a recently identified UfSP2 mutation that is associated with an autosomal dominant form of hip dysplasia. English AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC DEUBIQUITINATING ENZYMES CRYSTAL-STRUCTURE HUMAN ATG4B MECHANISM AUTOPHAGY UFM1 UBIQUITIN-FOLD-MODIFIER-1 RECOGNITION SPECIFICITY CATALYSIS Structure of Ubiquitin-fold Modifier 1-specific Protease UfSP2 Article 10.1074/jbc.M110.172171 1 JOURNAL OF BIOLOGICAL CHEMISTRY, v.286, no.12, pp.10248 - 10257 JOURNAL OF BIOLOGICAL CHEMISTRY 286 12 10248 10257 scie scopus 000288547000042 2-s2.0-79953194770 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article DEUBIQUITINATING ENZYMES CRYSTAL-STRUCTURE HUMAN ATG4B MECHANISM AUTOPHAGY UFM1 UBIQUITIN-FOLD-MODIFIER-1 RECOGNITION SPECIFICITY CATALYSIS