Please use this identifier to cite or link to this item: 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

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