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A novel approach to assess the ubiquitin‐fold modifier 1‐system in cells
Author(s) -
Ishimura Ryosuke,
Obata Miki,
Kageyama Shun,
Daniel Jens,
Tanaka Keiji,
Komatsu Masaaki
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12518
Subject(s) - endoplasmic reticulum , ubiquitin ligase , ubiquitin , ectopic expression , chemistry , microbiology and biotechnology , gene isoform , conjugate , biology , biochemistry , gene , mathematical analysis , mathematics
The ubiquitin‐fold modifier 1 ( UFM 1)‐system, a ubiquitin‐like protein conjugation system, is involved in the development of breast cancer and several hereditary neurological syndromes. However, the molecular mechanisms of UFM 1‐related pathogenesis remain unclear. Here, we show that in the absence of UFSP 2, a deconjugating enzyme for UFM 1, ectopic expression of both UFL 1 and UFBP 1, which serve as the E3‐ligase complex for the UFM 1‐system, dramatically increases UFM 1‐conjugate formation at the endoplasmic reticulum. Utilizing this system, we were able to attribute disease‐related isoforms of UBA 5, the E1 enzyme for UFM 1, to decreased UFM 1‐conjugate formation. Our procedure allows the assessment of UFM 1‐conjugate formation in cells and the identification of UFM 1‐targets, both of which are needed to clarify the pathophysiological role of the UFM 1‐system.