Open Access

Studies on the functional role of UFMylation in cells (Review)

  • Authors:
    • Rong Qin
    • Yu Tang
    • Yuhang Yuan
    • Fangyu Meng
    • Kepu Zheng
    • Xingyu Yang
    • Jiumei Zhao
    • Chuanhua Yang
  • View Affiliations

  • Published online on: May 2, 2025     https://doi.org/10.3892/mmr.2025.13556
  • Article Number: 191
  • Copyright: © Qin et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

Protein post‑translational modifications (PTMs) play crucial roles in various life activities and aberrant protein modifications are closely associated with numerous major human diseases. Ubiquitination, the first identified protein modification system, involves the covalent attachment of ubiquitin molecules to lysine residues of target proteins. UFMylation, a recently discovered ubiquitin‑like modification, shares similarities with ubiquitination. The precursor form of ubiquitin fold modifier 1 (UFM1) undergoes synthesis and cleavage by UFM1‑specific protease 1 or UFM1‑specific protease 2 to generate activated UFM1‑G83. Subsequently, UFM1‑G83 is activated by a specific E1‑like activase, UFM1‑activating enzyme 5. UFM1‑conjugating enzyme 1 and an E3‑like ligase, UFM1‑specific ligase 1, recognize the target protein and facilitate UFMylation, leading to the degradation of the target protein. Current knowledge regarding UFMylation remains limited. Previous studies have demonstrated that defects in the UFMylation pathway can result in embryonic lethality in mice and various human diseases, highlighting the critical biological functions of UFMylation. However, the precise mechanisms underlying UFMylation remain elusive. This present review aimed to summarize recent research advances in UFMylation, with the aim of providing novel insights and perspectives for future investigations into this essential protein modification system.
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July-2025
Volume 32 Issue 1

Print ISSN: 1791-2997
Online ISSN:1791-3004

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Copy and paste a formatted citation
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Spandidos Publications style
Qin R, Tang Y, Yuan Y, Meng F, Zheng K, Yang X, Zhao J and Yang C: Studies on the functional role of UFMylation in cells (Review). Mol Med Rep 32: 191, 2025.
APA
Qin, R., Tang, Y., Yuan, Y., Meng, F., Zheng, K., Yang, X. ... Yang, C. (2025). Studies on the functional role of UFMylation in cells (Review). Molecular Medicine Reports, 32, 191. https://doi.org/10.3892/mmr.2025.13556
MLA
Qin, R., Tang, Y., Yuan, Y., Meng, F., Zheng, K., Yang, X., Zhao, J., Yang, C."Studies on the functional role of UFMylation in cells (Review)". Molecular Medicine Reports 32.1 (2025): 191.
Chicago
Qin, R., Tang, Y., Yuan, Y., Meng, F., Zheng, K., Yang, X., Zhao, J., Yang, C."Studies on the functional role of UFMylation in cells (Review)". Molecular Medicine Reports 32, no. 1 (2025): 191. https://doi.org/10.3892/mmr.2025.13556