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Article ; Online: Corrigenda to "LUBAC-mediated linear ubiquitination: a crucial regulator of immune signaling".

Iwai, Kazuhiro

Proceedings of the Japan Academy. Series B, Physical and biological sciences

2021 Volume 97, Issue 4, Page(s) 210

Language	English
Publishing date	2021-03-31
Publishing country	Japan
Document type	Journal Article ; Published Erratum
ZDB-ID	161781-3
ISSN	1349-2896 ; 0386-2208
ISSN (online)	1349-2896
ISSN	0386-2208
DOI	10.2183/pjab.97.012
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Article ; Online: LUBAC-mediated linear ubiquitination: a crucial regulator of immune signaling.

Iwai, Kazuhiro

Proceedings of the Japan Academy. Series B, Physical and biological sciences

2021 Volume 97, Issue 3, Page(s) 120–133

Abstract: Ubiquitination is a reversible post-translational modification in which ubiquitin chains are conjugated to target proteins to modulate protein function. The type of ubiquitin chain determines the mode of protein regulation. It has been shown that ... ...

Abstract	Ubiquitination is a reversible post-translational modification in which ubiquitin chains are conjugated to target proteins to modulate protein function. The type of ubiquitin chain determines the mode of protein regulation. It has been shown that ubiquitin chains are formed via one of seven Lys residues in ubiquitin, and several types of ubiquitin chains are found in cells. We identified a new type of linear ubiquitin chain linked through the N-terminal Met of ubiquitin and assembled by the linear ubiquitin chain assembly complex (LUBAC), which is specific for linear chains. The discovery of linear ubiquitin chains and LUBAC is considered as a paradigm shift in ubiquitin research because linear ubiquitination is exclusive to animals, despite the existence of ubiquitination throughout eukaryotic kingdoms. Linear ubiquitination plays a critical role in immune signaling and cell death regulation. Dysregulation of LUBAC-mediated linear ubiquitination underlies various human diseases, including autoinflammation, autoimmunity, infection, and malignant tumors. This review summarizes the current status of linear ubiquitination research.
MeSH term(s)	Immunity ; Signal Transduction ; Ubiquitin/chemistry ; Ubiquitin/metabolism ; Ubiquitination
Chemical Substances	Ubiquitin
Language	English
Publishing date	2021-03-10
Publishing country	Japan
Document type	Journal Article
ZDB-ID	161781-3
ISSN	1349-2896 ; 0386-2208
ISSN (online)	1349-2896
ISSN	0386-2208
DOI	10.2183/pjab.97.007
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Article ; Online: Oxygen modulates iron homeostasis by switching iron sensing of NCOA4.

Kuno, Sota / Iwai, Kazuhiro

The Journal of biological chemistry

2023 Volume 299, Issue 5, Page(s) 104701

Abstract: To ensure proper utilization of iron and avoid its toxicity, cells are equipped with iron-sensing proteins to maintain cellular iron homeostasis. We showed previously that nuclear receptor coactivator 4 (NCOA4), a ferritin-specific autophagy adapter, ... ...

Abstract	To ensure proper utilization of iron and avoid its toxicity, cells are equipped with iron-sensing proteins to maintain cellular iron homeostasis. We showed previously that nuclear receptor coactivator 4 (NCOA4), a ferritin-specific autophagy adapter, intricately regulates the fate of ferritin; upon binding to Fe
MeSH term(s)	Iron/metabolism ; Oxygen/metabolism ; Nuclear Receptor Coactivators/genetics ; Ferritins/metabolism ; Transcription Factors/metabolism ; Homeostasis ; Ubiquitins/metabolism ; Autophagy
Chemical Substances	Iron (E1UOL152H7) ; Oxygen (S88TT14065) ; Nuclear Receptor Coactivators ; Ferritins (9007-73-2) ; Transcription Factors ; Ubiquitins
Language	English
Publishing date	2023-04-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104701
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Article ; Online: Discovery of linear ubiquitination, a crucial regulator for immune signaling and cell death.

Iwai, Kazuhiro

The FEBS journal

2020 Volume 288, Issue 4, Page(s) 1060–1069

Abstract: Ubiquitination is a reversible post-translational modification that regulates function of conjugated proteins by decorating with ubiquitin chains-polymer of ubiquitin-in most cases. The discovery of linear ubiquitin chains and the linear ubiquitin chain ... ...

Abstract	Ubiquitination is a reversible post-translational modification that regulates function of conjugated proteins by decorating with ubiquitin chains-polymer of ubiquitin-in most cases. The discovery of linear ubiquitin chains and the linear ubiquitin chain assembly complex (LUBAC) ubiquitin ligase complex can be considered as paradigm shift in the ubiquitin research because the linear ubiquitin chain is generated via the N-terminal Met of ubiquitin, although the other ubiquitin chains are generated via one of seven Lys residues in ubiquitin. Moreover, ubiquitination is distributed throughout eukaryotic kingdoms; however, no linear ubiquitination could be found in lower eukaryotes including yeasts. Although the involvement of ubiquitination in proteolysis is well-documented, linear ubiquitination plays crucial roles in immune signaling and cell death regulation. Moreover, dysregulation of LUBAC-mediated linear ubiquitination underlies various human diseases including autoinflammation and cancer. Here, I introduce how linear ubiquitination was discovered and outline a brief history of linear ubiquitination research.
MeSH term(s)	Animals ; Cell Death/immunology ; Humans ; Inflammation/immunology ; Inflammation/metabolism ; NF-kappa B/immunology ; NF-kappa B/metabolism ; Neoplasms/immunology ; Neoplasms/metabolism ; Signal Transduction/immunology ; Ubiquitin/immunology ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/immunology ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/immunology
Chemical Substances	NF-kappa B ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2020-07-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15471
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Article ; Online: LUBAC-mediated linear ubiquitination in tissue homeostasis and disease.

Sasaki, Katsuhiro / Iwai, Kazuhiro

Journal of biochemistry

2023 Volume 174, Issue 2, Page(s) 99–107

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 ...

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.
MeSH term(s)	Polyubiquitin/metabolism ; Ubiquitination ; Ubiquitin/genetics ; Ubiquitin/metabolism ; NF-kappa B/metabolism ; Homeostasis ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Polyubiquitin (120904-94-1) ; Ubiquitin ; NF-kappa B ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2023-07-27
Publishing country	England
Document type	Review ; Journal Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvad045
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Article ; Online: Role of linear ubiquitination in inflammatory responses and tissue homeostasis.

Sasaki, Katsuhiro / Iwai, Kazuhiro

International immunology

2022 Volume 35, Issue 1, Page(s) 19–25

Abstract: Polyubiquitination is a post-translational modification involved in a wide range of immunological events, including inflammatory responses, immune cell differentiation, and development of inflammatory diseases. The versatile functions of ... ...

Abstract	Polyubiquitination is a post-translational modification involved in a wide range of immunological events, including inflammatory responses, immune cell differentiation, and development of inflammatory diseases. The versatile functions of polyubiquitination are based on different types of ubiquitin linkage, which enable various UBD (ubiquitin binding domain)-containing adaptor proteins to associate and induce distinct biological outputs. A unique and atypical type of polyubiquitin chain comprising a conjugation between the N-terminal methionine of the proximal ubiquitin moiety and the C-terminal glycine of the distal ubiquitin moiety, referred to as a linear or M1-linked ubiquitin chain, has been studied exclusively within the field of immunology because it is distinct from other polyubiquitin forms: linear ubiquitin chains are generated predominantly by various inflammatory stimulants, including tumor necrosis factor-α (TNF-α) and interleukin-1β (IL-1β), and act as a critical modulator of transient and optimal signal transduction. Moreover, accumulating evidence suggests that linear ubiquitin chains are of physiological significance. Dysregulation of linear ubiquitination triggers chronic inflammation and immunodeficiency via downregulation of linear ubiquitin-dependent nuclear factor-kappa B (NF-κB) signaling and by triggering TNF-α-induced cell death, suggesting that linear ubiquitination is a homeostatic regulator of tissue-specific functions. In this review, we focus on our current understating of the molecular and cellular mechanisms by which linear ubiquitin chains control inflammatory environments. Furthermore, we review the role of linear ubiquitination on T cell development, differentiation, and function, thereby providing insight into its direct association with maintaining the immune system.
MeSH term(s)	Polyubiquitin/metabolism ; Tumor Necrosis Factor-alpha/metabolism ; Ubiquitination ; Ubiquitin/metabolism ; NF-kappa B/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Homeostasis
Chemical Substances	Polyubiquitin (120904-94-1) ; Tumor Necrosis Factor-alpha ; Ubiquitin ; NF-kappa B ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2022-09-22
Publishing country	England
Document type	Review ; Journal Article
ZDB-ID	1013745-2
ISSN	1460-2377 ; 0953-8178
ISSN (online)	1460-2377
ISSN	0953-8178
DOI	10.1093/intimm/dxac047
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Article ; Online: Regulation of cellular iron metabolism: Iron-dependent degradation of IRP by SCF

Iwai, Kazuhiro

Free radical biology & medicine

2018 Volume 133, Page(s) 64–68

Abstract: Because of essentiality and toxicity of iron in our body, iron metabolism is tightly regulated in cells. In mammalian cells, iron regulatory protein 1 and 2 (IRP1 and IRP2) are the central regulators of cellular iron metabolism. IRPs regulate iron ... ...

Abstract	Because of essentiality and toxicity of iron in our body, iron metabolism is tightly regulated in cells. In mammalian cells, iron regulatory protein 1 and 2 (IRP1 and IRP2) are the central regulators of cellular iron metabolism. IRPs regulate iron metabolism by interacting with the RNA stem-loop structures, iron-responsive elements (IREs), found on the transcripts encoding proteins involved in iron metabolism only in iron depleted condition. It is also well-known that the ubiquitin system plays central roles in cellular iron regulation because both IRPs having the IRE binding activity are recognized and ubiquitinated by the SCF
MeSH term(s)	Animals ; F-Box Proteins/genetics ; F-Box Proteins/metabolism ; Humans ; Inverted Repeat Sequences/genetics ; Iron/metabolism ; Iron Regulatory Protein 1/genetics ; Iron Regulatory Protein 1/metabolism ; Iron Regulatory Protein 2/genetics ; Iron Regulatory Protein 2/metabolism ; Iron-Regulatory Proteins/genetics ; Iron-Regulatory Proteins/metabolism ; RNA/genetics ; RNA/metabolism ; SKP Cullin F-Box Protein Ligases/genetics ; SKP Cullin F-Box Protein Ligases/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligase Complexes/genetics ; Ubiquitin-Protein Ligase Complexes/metabolism
Chemical Substances	F-Box Proteins ; FBXL5 protein, human ; Iron-Regulatory Proteins ; Ubiquitin ; RNA (63231-63-0) ; Iron (E1UOL152H7) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; SKP Cullin F-Box Protein Ligases (EC 2.3.2.27) ; Iron Regulatory Protein 1 (EC 4.2.1.3) ; Iron Regulatory Protein 2 (EC 4.2.1.3)
Language	English
Publishing date	2018-09-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2018.09.011
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Article ; Online: Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination: Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase.

Fuseya, Yasuhiro / Iwai, Kazuhiro

Cells

2021 Volume 10, Issue 10

Abstract: The ubiquitin system modulates protein functions by decorating target proteins with ubiquitin chains in most cases. Several types of ubiquitin chains exist, and chain type determines the mode of regulation of conjugated proteins. LUBAC is a ubiquitin ... ...

Abstract	The ubiquitin system modulates protein functions by decorating target proteins with ubiquitin chains in most cases. Several types of ubiquitin chains exist, and chain type determines the mode of regulation of conjugated proteins. LUBAC is a ubiquitin ligase complex that specifically generates N-terminally Met1-linked linear ubiquitin chains. Although linear ubiquitin chains are much less abundant than other types of ubiquitin chains, they play pivotal roles in cell survival, proliferation, the immune response, and elimination of bacteria by selective autophagy. Because linear ubiquitin chains regulate inflammatory responses by controlling the proinflammatory transcription factor NF-κB and programmed cell death (including apoptosis and necroptosis), abnormal generation of linear chains can result in pathogenesis. LUBAC consists of HOIP, HOIL-1L, and SHARPIN; HOIP is the catalytic center for linear ubiquitination. LUBAC is unique in that it contains two different ubiquitin ligases, HOIP and HOIL-1L, in the same ligase complex. Furthermore, LUBAC constitutively interacts with the deubiquitinating enzymes (DUBs) OTULIN and CYLD, which cleave linear ubiquitin chains generated by LUBAC. In this review, we summarize the current status of linear ubiquitination research, and we discuss the intricate regulation of LUBAC-mediated linear ubiquitination by coordinate function of the HOIP and HOIL-1L ligases and OTULIN. Furthermore, we discuss therapeutic approaches to targeting LUBAC-mediated linear ubiquitin chains.
MeSH term(s)	Animals ; Deubiquitinating Enzymes/metabolism ; Disease ; Humans ; Molecular Targeted Therapy ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Deubiquitinating Enzymes (EC 3.4.19.12)
Language	English
Publishing date	2021-10-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10102706
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Article ; Online: Linear ubiquitination-induced necrotic tumor remodeling elicits immune evasion.

Sasaki, Katsuhiro / Hayamizu, Yoshie / Murakami, Ryuji / Toi, Masakazu / Iwai, Kazuhiro

FEBS letters

2023 Volume 597, Issue 9, Page(s) 1193–1212

Abstract: Tumor-elicited inflammation confers tumorigenic properties, including cell death resistance, proliferation, or immune evasion. To focus on inflammatory signaling in tumors, we investigated linear ubiquitination, which enhances the nuclear factor-κB ... ...

Abstract	Tumor-elicited inflammation confers tumorigenic properties, including cell death resistance, proliferation, or immune evasion. To focus on inflammatory signaling in tumors, we investigated linear ubiquitination, which enhances the nuclear factor-κB signaling pathway and prevents extrinsic programmed cell death under inflammatory environments. Here, we showed that linear ubiquitination was augmented especially in tumor cells around a necrotic core. Linear ubiquitination allowed melanomas to tolerate the hostile tumor microenvironment and to extend a necrosis-containing morphology. Loss of linear ubiquitination resulted in few necrotic lesions and growth regression, further leading to repression of innate anti-PD-1 therapy resistance signatures in melanoma as well as activation of interferon responses and antigen presentation that promote immune-mediated tumor eradication. Collectively, linear ubiquitination promotes tumor-specific tissue remodeling and the ensuing immune evasion.
MeSH term(s)	Humans ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Immune Evasion ; Ubiquitination ; NF-kappa B/metabolism ; Necrosis ; Neoplasms ; Tumor Microenvironment
Chemical Substances	Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; NF-kappa B
Language	English
Publishing date	2023-04-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14623
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Article ; Online: Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination

Yasuhiro Fuseya / Kazuhiro Iwai

Cells, Vol 10, Iss 2706, p

Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase

2021 Volume 2706

Abstract	The ubiquitin system modulates protein functions by decorating target proteins with ubiquitin chains in most cases. Several types of ubiquitin chains exist, and chain type determines the mode of regulation of conjugated proteins. LUBAC is a ubiquitin ligase complex that specifically generates N-terminally Met1-linked linear ubiquitin chains. Although linear ubiquitin chains are much less abundant than other types of ubiquitin chains, they play pivotal roles in cell survival, proliferation, the immune response, and elimination of bacteria by selective autophagy. Because linear ubiquitin chains regulate inflammatory responses by controlling the proinflammatory transcription factor NF-κB and programmed cell death (including apoptosis and necroptosis), abnormal generation of linear chains can result in pathogenesis. LUBAC consists of HOIP, HOIL-1L, and SHARPIN; HOIP is the catalytic center for linear ubiquitination. LUBAC is unique in that it contains two different ubiquitin ligases, HOIP and HOIL-1L, in the same ligase complex. Furthermore, LUBAC constitutively interacts with the deubiquitinating enzymes (DUBs) OTULIN and CYLD, which cleave linear ubiquitin chains generated by LUBAC. In this review, we summarize the current status of linear ubiquitination research, and we discuss the intricate regulation of LUBAC-mediated linear ubiquitination by coordinate function of the HOIP and HOIL-1L ligases and OTULIN. Furthermore, we discuss therapeutic approaches to targeting LUBAC-mediated linear ubiquitin chains.
Keywords	ubiquitin ; linear ubiquitin chains ; LUBAC ; HOIL-1L ; HOIP ; OTULIN ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-10-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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