Journal
FEBS LETTERS
Volume 591, Issue 1, Pages 196-204Publisher
WILEY
DOI: 10.1002/1873-3468.12518
Keywords
encephalopathy; ubiquitin-like modifier; UFM1
Funding
- Japan Society for the Promotion of Science [JPPE1611]
- Japan Society for the Promotion of Science
- Takeda Science Foundation
- [JP16J07037]
- [JP25111006]
- [JP26253019]
- Grants-in-Aid for Scientific Research [26000014, 16J07037] Funding Source: KAKEN
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The ubiquitin-fold modifier 1 (UFM1)-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 UFM1-related pathogenesis remain unclear. Here, we show that in the absence of UFSP2, a deconjugating enzyme for UFM1, ectopic expression of both UFL1 and UFBP1, which serve as the E3-ligase complex for the UFM1-system, dramatically increases UFM1-conjugate formation at the endoplasmic reticulum. Utilizing this system, we were able to attribute disease-related isoforms of UBA5, the E1 enzyme for UFM1, to decreased UFM1-conjugate formation. Our procedure allows the assessment of UFM1-conjugate formation in cells and the identification of UFM1-targets, both of which are needed to clarify the pathophysiological role of the UFM1-system.
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