LUBAC-mediated linear ubiquitination in tissue homeostasis and disease.
| Title: | LUBAC-mediated linear ubiquitination in tissue homeostasis and disease. |
|---|---|
| Authors: | Sasaki, Katsuhiro1 (AUTHOR) katsuhiro.sasaki@mcp.med.kyoto-u.ac.jp, Iwai, Kazuhiro1 (AUTHOR) |
| Source: | Journal of Biochemistry. Aug2023, Vol. 174 Issue 2, p99-107. 9p. |
| Subject Terms: | *PROTEOLYSIS, *UBIQUITINATION, *APOPTOSIS, *HOMEOSTASIS, *DIFFUSE large B-cell lymphomas, *ADAPTOR proteins |
| Abstract: | In addition to its role in the ubiquitin–proteasome system of protein degradation, polyubiquitination is involved in the regulation of intracellular events. Depending on the type of ubiquitin–ubiquitin linkage used, polyubiquitin can assume several types of structures. The spatiotemporal dynamics of polyubiquitin involve multiple adaptor proteins and induce different downstream outputs. Linear ubiquitination, in which the N-terminal methionine on the acceptor ubiquitin serves as the site for ubiquitin–ubiquitin conjugation, is a rare and atypical type of polyubiquitin modification. The production of linear ubiquitin chains is dependent on various external inflammatory stimuli and leads to the transient activation of the downstream NF-κB signalling pathway. This in turn suppresses extrinsic programmed cell death signals and protects cells from activation-induced cell death under inflammatory conditions. Recent evidence has revealed the role of linear ubiquitination in various biological processes under both physiological and pathological conditions. This led us to propose that linear ubiquitination may be pivotal in the 'inflammatory adaptation' of cells, and consequently in tissue homeostasis and inflammatory disease. In this review, we focused on the physiological and pathophysiological roles of linear ubiquitination in vivo in response to a changing inflammatory microenvironment. [ABSTRACT FROM AUTHOR] |
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| Items | – Name: Title Label: Title Group: Ti Data: LUBAC-mediated linear ubiquitination in tissue homeostasis and disease. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Sasaki%2C+Katsuhiro%22">Sasaki, Katsuhiro</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> katsuhiro.sasaki@mcp.med.kyoto-u.ac.jp</i><br /><searchLink fieldCode="AR" term="%22Iwai%2C+Kazuhiro%22">Iwai, Kazuhiro</searchLink><relatesTo>1</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biochemistry%22">Journal of Biochemistry</searchLink>. Aug2023, Vol. 174 Issue 2, p99-107. 9p. – Name: Subject Label: Subject Terms Group: Su Data: *<searchLink fieldCode="DE" term="%22PROTEOLYSIS%22">PROTEOLYSIS</searchLink><br />*<searchLink fieldCode="DE" term="%22UBIQUITINATION%22">UBIQUITINATION</searchLink><br />*<searchLink fieldCode="DE" term="%22APOPTOSIS%22">APOPTOSIS</searchLink><br />*<searchLink fieldCode="DE" term="%22HOMEOSTASIS%22">HOMEOSTASIS</searchLink><br />*<searchLink fieldCode="DE" term="%22DIFFUSE+large+B-cell+lymphomas%22">DIFFUSE large B-cell lymphomas</searchLink><br />*<searchLink fieldCode="DE" term="%22ADAPTOR+proteins%22">ADAPTOR proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: In addition to its role in the ubiquitin–proteasome system of protein degradation, polyubiquitination is involved in the regulation of intracellular events. Depending on the type of ubiquitin–ubiquitin linkage used, polyubiquitin can assume several types of structures. The spatiotemporal dynamics of polyubiquitin involve multiple adaptor proteins and induce different downstream outputs. Linear ubiquitination, in which the N-terminal methionine on the acceptor ubiquitin serves as the site for ubiquitin–ubiquitin conjugation, is a rare and atypical type of polyubiquitin modification. The production of linear ubiquitin chains is dependent on various external inflammatory stimuli and leads to the transient activation of the downstream NF-κB signalling pathway. This in turn suppresses extrinsic programmed cell death signals and protects cells from activation-induced cell death under inflammatory conditions. Recent evidence has revealed the role of linear ubiquitination in various biological processes under both physiological and pathological conditions. This led us to propose that linear ubiquitination may be pivotal in the 'inflammatory adaptation' of cells, and consequently in tissue homeostasis and inflammatory disease. In this review, we focused on the physiological and pathophysiological roles of linear ubiquitination in vivo in response to a changing inflammatory microenvironment. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Biochemistry is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1093/jb/mvad045 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 9 StartPage: 99 Subjects: – SubjectFull: PROTEOLYSIS Type: general – SubjectFull: UBIQUITINATION Type: general – SubjectFull: APOPTOSIS Type: general – SubjectFull: HOMEOSTASIS Type: general – SubjectFull: DIFFUSE large B-cell lymphomas Type: general – SubjectFull: ADAPTOR proteins Type: general Titles: – TitleFull: LUBAC-mediated linear ubiquitination in tissue homeostasis and disease. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Sasaki, Katsuhiro – PersonEntity: Name: NameFull: Iwai, Kazuhiro IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 08 Text: Aug2023 Type: published Y: 2023 Identifiers: – Type: issn-print Value: 0021924X Numbering: – Type: volume Value: 174 – Type: issue Value: 2 Titles: – TitleFull: Journal of Biochemistry Type: main |
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