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Conformational stabilization of optineurin by the dynamic interaction of linear polyubiquitin

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Title: Conformational stabilization of optineurin by the dynamic interaction of linear polyubiquitin
Authors: Kitamura, Akira Browse this author →KAKEN DB
Numazawa, Rika Browse this author
Kinjo, Masataka Browse this author →KAKEN DB
Keywords: Optineurin
Protein aggregation
Issue Date: 25-Jun-2021
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 559
Start Page: 203
End Page: 209
Publisher DOI: 10.1016/j.bbrc.2021.04.103
Abstract: Optineurin produces intracellular multi-functions involving autophagy, vesicular trafficking, and negative regulation of inflammation signaling through interaction with various proteins such as ATG8/LC3, Rab8, and polyubiquitin. Optineurin is a component of cytoplasmic inclusion bodies (IBs) in motor neurons from amyotrophic lateral sclerosis (ALS), and its mutation E478G, has been identified in patients with ALS. However, the mechanism by which polyubiquitin binding modulates the interaction partners of OPTN and ALS-associated IB formation is still unclear. To address this issue, we analyzed the interaction of Optineurin with Rab8 and LC3 in the absence and presence of linear polyubiquitin chains using fluorescence cross-correlation spectroscopy and IB formation efficiency of the E478G mutant of Optineurin during Rab8 depletion using fluorescence microscopy. Here, we hypothesize that linear polyubiquitin binding to Optineurin dynamically induces LC3 association and Rab8 dissociation, likely through a conformational change of Optineurin, and the dynamic conformational change may prevent the aggregate formation of mutant Optineurin.
Rights: ©2021. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
Type: article (author version)
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 北村 朗

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