Version 1
: Received: 15 September 2024 / Approved: 16 September 2024 / Online: 16 September 2024 (09:59:19 CEST)
How to cite:
Mirzadeh, A.; Kazemi, M.; Rouiller, I. Molecular Mechanism of Processing Ubiquitinated Substrates by p97 and Its Main Cofactors. Preprints2024, 2024091194. https://doi.org/10.20944/preprints202409.1194.v1
Mirzadeh, A.; Kazemi, M.; Rouiller, I. Molecular Mechanism of Processing Ubiquitinated Substrates by p97 and Its Main Cofactors. Preprints 2024, 2024091194. https://doi.org/10.20944/preprints202409.1194.v1
Mirzadeh, A.; Kazemi, M.; Rouiller, I. Molecular Mechanism of Processing Ubiquitinated Substrates by p97 and Its Main Cofactors. Preprints2024, 2024091194. https://doi.org/10.20944/preprints202409.1194.v1
APA Style
Mirzadeh, A., Kazemi, M., & Rouiller, I. (2024). Molecular Mechanism of Processing Ubiquitinated Substrates by p97 and Its Main Cofactors. Preprints. https://doi.org/10.20944/preprints202409.1194.v1
Chicago/Turabian Style
Mirzadeh, A., Mohsen Kazemi and Isabelle Rouiller. 2024 "Molecular Mechanism of Processing Ubiquitinated Substrates by p97 and Its Main Cofactors" Preprints. https://doi.org/10.20944/preprints202409.1194.v1
Abstract
p97(also known as Cdc48 or VCP) is a conserved AAA+ ATPase that plays a key role in diverse cellular pathways and processes. p97 segregates damaged or misfolded substrates from cellular organelles or membranes in corporation with its cofactors. These cofactors regulate p97’s function by its directing to different cellular pathways and have diverse effect on p97´s conformation. Recently, several high-resolution structures of substrate-engaged p97 in complex with cofactors have been resolved, providing structural insights into the molecular mechanism of substrate processing. In this review, we present a comprehensive overview of how p97 in complex with substrate recruiting and substrate processing cofactors recognize, extract, translocate, unfold and release ubiquitinated substrates.
Keywords
p97; cofactors; substrate processing; Single particle cryo_electron microscopy
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
