Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 633, Issue -, Pages 61-63Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.08.093
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- National Research Foundation of Korea [NRF-2005-084-C00025]
- Korea Research Institute of Standards and Science [NRISS-2022-GP2022-0003]
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This article summarizes the recent progress in the understanding of the tumor-suppressive and tumorigenic functions of ufmylation, as well as the development of therapeutic drugs against ufmylation-associated cancer.
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. (c) 2022 Elsevier Inc. All rights reserved.
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