Format

Send to

Choose Destination
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.

Author information

1
Department of Biochemistry, Niigata University Graduate School of Medical and Dental Sciences, Japan.
2
Laboratory of Protein Metabolism, The Tokyo Metropolitan Institute of Medical Science, Japan.

Abstract

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.

KEYWORDS:

UFM1; encephalopathy; ubiquitin-like modifier

PMID:
27926783
DOI:
10.1002/1873-3468.12518
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center