Emerging role of protein modification by UFM1 in cancer.

Biochem Biophys Res Commun

School of Biological Sciences, Seoul National University, Seoul, 08826, South Korea; Biometrology Group, Korea Research Institute of Standards and Science (KRISS), Daejeon, 34113, South Korea.

Published: December 2022

AI Article Synopsis

  • Ubiquitin-fold modifier 1 (UFM1) is a newly discovered protein similar to ubiquitin, which modifies other proteins through a specific enzyme process.
  • UFM1's modification, called ufmylation, can be reversed by specific enzymes known as UFM1-specific proteases.
  • Current research focuses on the roles of ufmylation in cancer, highlighting its potential both in suppressing and promoting tumor growth, as well as the development of new treatment options for cancers related to ufmylation.

Article Abstract

Ubiquitin-fold modifier 1 (UFM1) is a newly identified ubiquitin-like protein. Like ubiquitin, UFM1 is conjugated to its target proteins through a three-step enzyme system: UBA5 (E1), UFC1 (E2), and UFL1 (E3), but with an additional essential component, UFBP1. This protein modification by UFM1 (ufmylation) can be reversed by UFM1-specific proteases (UFSPs). So far only a handful of target proteins for ufmylation have been identified, and they are mostly associated with either promotion or suppression of tumorigenesis. Here, we summarize the recent progress in the knowledge of tumor-suppressive and tumorigenic functions of ufmylation as well as in the development of therapeutic drugs against ufmylation-associated cancer.

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Source
http://dx.doi.org/10.1016/j.bbrc.2022.08.093DOI Listing

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