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FEBS Lett. 2017 Jan;591(1):196-204. doi: 10.1002/1873-3468.12518. Epub 2016 Dec 20.

A novel approach to assess the ubiquitin-fold modifier 1-system in cells.

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Department of Biochemistry, Niigata University Graduate School of Medical and Dental Sciences, Japan.
Laboratory of Protein Metabolism, The Tokyo Metropolitan Institute of Medical Science, Japan.


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.


UFM1; encephalopathy; ubiquitin-like modifier

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