Bombyx mori UFL1 facilitates BmNPV proliferation by regulating host cell apoptosis through PERK
Yijun Zheng1, Haonan Meng2, Xiaochun Jiang2
1School of Chinese Materia Medica, Tianjin University of Traditional Chinese Medicine, Tianjin, China.
Abstract:
Ubiquitin-fold modifier 1 (UFM1) is attached to protein substrates through the sequential activity of an E1 (UBA5)-E2 (UFC1)-E3 (UFL1) cascade. UFL1 is the E3 ligase for UFMylation in vertebrates. However, there have been no studies on UFL1 in silkworm to date. In this study, we identified a UFL1 ortholog in Bombyx mori genome. Spatio-temporal expression profiles showed that BmUFL1 expression was high in the midgut, epidermis, and testis and in the pupa-adult stage. BmUFL1 knockdown inhibited B. mori nucleopolyhedrovirus (BmNPV) proliferation, while BmUFL1 overexpression promoted BmNPV proliferation. Mechanically, protein kinase RNA-like endoplasmic reticulum kinase (PERK) signaling and cell apoptosis are involved in BmUFL1-regulated BmNPV proliferation. Overall, these results suggest that BmUFL1 facilitates BmNPV proliferation in silkworm.
More Related Videos
10:50Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
Published on: April 24, 2021
07:15Mechanism of Kemeng Fang's Inhibition of Podocyte Apoptosis in Rats with Membranous Nephropathy through the PI3K/AKT Signaling Pathway
Published on: August 23, 2024
Related Concept Videos
Abnormal Proliferation
The Intrinsic Apoptotic Pathway
The Extrinsic Apoptotic Pathway
Caspases
Negative Regulator Molecules
NF-κB-dependent Signaling Pathway
NF-κB-dependent Signaling Mechanism
The...
