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http://223.31.159.10:8080/jspui/handle/123456789/1695| Title: | UFMylation: Exploring a lesser known post translational modification |
| Authors: | Sharma, Rohit Chirom, Oceania Mujib, Abdul Prasad, Manoj Prasad, Ashish |
| Keywords: | PTM UBLs UFMylation Ubiquitin ER homeostasis |
| Issue Date: | 2025 |
| Publisher: | Elsevier B.V. |
| Citation: | Plant Science, 354: 112435 |
| Abstract: | Ubiquitination is a highly conserved post-translational modification (PTM) in which ubiquitin (Ub) is covalently attached to substrate proteins resulting in the alteration of protein structure, function, and stability. Another class of PTM mediated by ubiquitin-like proteins (UBLs) has gained significant attention among researchers in recent years. This article focuses on one such UBL-mediated PTM i.e. UFMylation. The enzymatic mechanism of UFMylation is similar to ubiquitination, involving three steps regulated by three different enzymes. In plants, reports suggest that UFMylation is predominantly involved in maintaining ER homeostasis including ER-phagy. However, studies related to this PTM are limited and future studies might reveal other molecular pathways regulated by UFMylation. |
| Description: | Accepted date: 18 February 2025 |
| URI: | https://www.sciencedirect.com/science/article/pii/S0168945225000536?via%3Dihub http://223.31.159.10:8080/jspui/handle/123456789/1695 |
| ISSN: | 1873-2259 0168-9452 |
| Appears in Collections: | Institutional Publications |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Prasad M_2025_1.pdf Restricted Access | 1.66 MB | Adobe PDF | View/Open Request a copy |
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