TSG101 Physically Interacts with Linear Ubiquitin Chain Assembly Complex (LUBAC) and Upregulates the TNFα-Induced NF-κB Activation

Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1- linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimu...

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Published inMolecules and cells Vol. 46; no. 7; pp. 430 - 440
Main Authors Kim, Eunju, Cho, Hyunchu, Lee, Gaeul, Baek, Heawon, Lee, In Young, Choi, Eui-Ju
Format Journal Article
LanguageEnglish
Published United States Korean Society for Molecular and Cellular Biology 31.07.2023
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Abstract Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1- linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimuli. Here, we found that tumor susceptibility gene (TSG101) physically interacts with HOIP, a catalytic component of LUBAC, and potentiates LUBAC activity. Depletion of TSG101 expression by RNA interference decreased TNFα-induced linear ubiquitination and the formation of TNFα receptor 1 signaling complex (TNFRSC). Furthermore, TSG101 facilitated the TNFα-induced stimulation of the NF-κB pathway. Thus, we suggest that TSG101 functions as a positive modulator of HOIP that mediates TNFα-induced NF-κB signaling pathway.
AbstractList Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1-linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimuli. Here, we found that tumor susceptibility gene (TSG101) physically interacts with HOIP, a catalytic component of LUBAC, and potentiates LUBAC activity. Depletion of TSG101 expression by RNA interference decreased TNFα-induced linear ubiquitination and the formation of TNFα receptor 1 signaling complex (TNF-RSC). Furthermore, TSG101 facilitated the TNFα-induced stimulation of the NF-κB pathway. Thus, we suggest that TSG101 functions as a positive modulator of HOIP that mediates TNFα-induced NF-κB signaling pathway.
Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1- linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimuli. Here, we found that tumor susceptibility gene (TSG101) physically interacts with HOIP, a catalytic component of LUBAC, and potentiates LUBAC activity. Depletion of TSG101 expression by RNA interference decreased TNFα-induced linear ubiquitination and the formation of TNFα receptor 1 signaling complex (TNFRSC). Furthermore, TSG101 facilitated the TNFα-induced stimulation of the NF-κB pathway. Thus, we suggest that TSG101 functions as a positive modulator of HOIP that mediates TNFα-induced NF-κB signaling pathway.
Author Kim, Eunju
Lee, In Young
Choi, Eui-Ju
Lee, Gaeul
Baek, Heawon
Cho, Hyunchu
AuthorAffiliation 2 GNT Science & Technology Center for Health, GNT Pharma Co., Ltd., Yongin 17096, Korea
1 Laboratory of Cell Death and Human Diseases, Department of Life Sciences, Korea University, Seoul 02841, Korea
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Cites_doi 10.1038/ncb1821
10.1038/nature09814
10.1016/S0092-8674(00)81111-3
10.1016/j.celrep.2017.09.031
10.1038/ng0897-330
10.1128/MCB.19.5.3588
10.1038/embor.2012.105
10.1074/jbc.M109.072256
10.1016/j.molcel.2014.03.016
10.1073/pnas.93.24.13973
10.1016/S1074-7613(00)80252-6
10.1073/pnas.98.4.1619
10.1034/j.1600-0854.2000.010307.x
10.1038/nature09816
10.1016/S0092-8674(01)00434-2
10.1111/gtc.12128
10.3390/cancers12020450
10.1073/pnas.0932599100
10.1016/j.cell.2009.03.007
10.1038/sj.emboj.7601360
10.1038/nature09815
10.1016/j.molcel.2016.08.001
10.7554/eLife.03464
10.1016/j.molcel.2014.03.018
10.1074/jbc.C800128200
10.1038/emboj.2012.217
10.15252/embj.201694300
10.1016/j.celrep.2016.07.086
10.1038/nature12638
10.1016/j.molcel.2009.10.013
10.1016/j.celrep.2014.08.066
10.1016/j.molcel.2019.01.022
10.1016/j.celrep.2018.03.112
10.1038/nature16511
10.1016/j.cell.2013.05.014
10.1093/emboj/21.10.2397
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Issue 7
Keywords nuclear factor-κB
tumor susceptibility gene 101
linear ubiquitin chain assembly complex
tumor necrosis factor α
HOIL-1-interacting protein
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0
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References Keusekotten (10.14348/molcells.2023.0026_bib12) 2013; 153
Vince (10.14348/molcells.2023.0026_bib37) 2009; 284
Babst (10.14348/molcells.2023.0026_bib1) 2000; 1
Feng (10.14348/molcells.2023.0026_bib4) 2000; 60
Liu (10.14348/molcells.2023.0026_bib21) 2017; 21
Schaeffer (10.14348/molcells.2023.0026_bib28) 2014; 54
Stieglitz (10.14348/molcells.2023.0026_bib32) 2013; 503
Pornillos (10.14348/molcells.2023.0026_bib25) 2002; 21
Kirisako (10.14348/molcells.2023.0026_bib13) 2006; 25
Ferraiuolo (10.14348/molcells.2023.0026_bib5) 2020; 12
Li (10.14348/molcells.2023.0026_bib18) 1996; 85
Li (10.14348/molcells.2023.0026_bib19) 2001; 98
Katzmann (10.14348/molcells.2023.0026_bib11) 2001; 106
Lu (10.14348/molcells.2023.0026_bib22) 2003; 100
Kupka (10.14348/molcells.2023.0026_bib15) 2016; 16
Tokunaga (10.14348/molcells.2023.0026_bib35) 2009; 11
Lee (10.14348/molcells.2023.0026_bib17) 2019; 73
Gerlach (10.14348/molcells.2023.0026_bib7) 2011; 471
Li (10.14348/molcells.2023.0026_bib20) 1999; 19
Elliott (10.14348/molcells.2023.0026_bib3) 2014; 54
Takiuchi (10.14348/molcells.2023.0026_bib33) 2014; 19
Lechtenberg (10.14348/molcells.2023.0026_bib16) 2016; 529
Ponting (10.14348/molcells.2023.0026_bib24) 1997; 75
Koonin (10.14348/molcells.2023.0026_bib14) 1997; 16
Smit (10.14348/molcells.2023.0026_bib30) 2012; 31
Hsu (10.14348/molcells.2023.0026_bib9) 1996; 4
Varfolomeev (10.14348/molcells.2023.0026_bib36) 2008; 283
Rickard (10.14348/molcells.2023.0026_bib27) 2014; 3
Stieglitz (10.14348/molcells.2023.0026_bib31) 2012; 13
Elliott (10.14348/molcells.2023.0026_bib2) 2016; 63
Ikeda (10.14348/molcells.2023.0026_bib10) 2011; 471
Wagner (10.14348/molcells.2023.0026_bib38) 2016; 35
Tokunaga (10.14348/molcells.2023.0026_bib34) 2011; 471
Peltzer (10.14348/molcells.2023.0026_bib23) 2014; 9
Fujita (10.14348/molcells.2023.0026_bib6) 2018; 23
Rahighi (10.14348/molcells.2023.0026_bib26) 2009; 136
Haas (10.14348/molcells.2023.0026_bib8) 2009; 36
Shu (10.14348/molcells.2023.0026_bib29) 1996; 93
References_xml – volume: 11
  start-page: 123
  year: 2009
  ident: 10.14348/molcells.2023.0026_bib35
  article-title: Involvement of linear polyubiquitylation of NEMO in NF-κB activation
  publication-title: Nat. Cell Biol.
  doi: 10.1038/ncb1821
  contributor:
    fullname: Tokunaga
– volume: 471
  start-page: 637
  year: 2011
  ident: 10.14348/molcells.2023.0026_bib10
  article-title: SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
  publication-title: Nature
  doi: 10.1038/nature09814
  contributor:
    fullname: Ikeda
– volume: 85
  start-page: 319
  year: 1996
  ident: 10.14348/molcells.2023.0026_bib18
  article-title: Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81111-3
  contributor:
    fullname: Li
– volume: 21
  start-page: 27
  year: 2017
  ident: 10.14348/molcells.2023.0026_bib21
  article-title: Structural insights into SHARPIN-mediated activation of HOIP for the linear ubiquitin chain assembly
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2017.09.031
  contributor:
    fullname: Liu
– volume: 16
  start-page: 330
  year: 1997
  ident: 10.14348/molcells.2023.0026_bib14
  article-title: TSG101 may be the prototype of a class of dominant negative ubiquitin regulators
  publication-title: Nat. Genet.
  doi: 10.1038/ng0897-330
  contributor:
    fullname: Koonin
– volume: 19
  start-page: 3588
  year: 1999
  ident: 10.14348/molcells.2023.0026_bib20
  article-title: Yeast mutants affecting possible quality control of plasma membrane proteins
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.19.5.3588
  contributor:
    fullname: Li
– volume: 13
  start-page: 840
  year: 2012
  ident: 10.14348/molcells.2023.0026_bib31
  article-title: LUBAC synthesizes linear ubiquitin chains via a thioester intermediate
  publication-title: EMBO Rep.
  doi: 10.1038/embor.2012.105
  contributor:
    fullname: Stieglitz
– volume: 284
  start-page: 35906
  year: 2009
  ident: 10.14348/molcells.2023.0026_bib37
  article-title: TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-κB and to prevent TNF-induced apoptosis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.072256
  contributor:
    fullname: Vince
– volume: 54
  start-page: 349
  year: 2014
  ident: 10.14348/molcells.2023.0026_bib28
  article-title: Binding of OTULIN to the PUB domain of HOIP controls NF-κB signaling
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2014.03.016
  contributor:
    fullname: Schaeffer
– volume: 93
  start-page: 13973
  year: 1996
  ident: 10.14348/molcells.2023.0026_bib29
  article-title: The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.93.24.13973
  contributor:
    fullname: Shu
– volume: 4
  start-page: 387
  year: 1996
  ident: 10.14348/molcells.2023.0026_bib9
  article-title: TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
  publication-title: Immunity
  doi: 10.1016/S1074-7613(00)80252-6
  contributor:
    fullname: Hsu
– volume: 98
  start-page: 1619
  year: 2001
  ident: 10.14348/molcells.2023.0026_bib19
  article-title: A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.98.4.1619
  contributor:
    fullname: Li
– volume: 1
  start-page: 248
  year: 2000
  ident: 10.14348/molcells.2023.0026_bib1
  article-title: Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
  publication-title: Traffic
  doi: 10.1034/j.1600-0854.2000.010307.x
  contributor:
    fullname: Babst
– volume: 471
  start-page: 591
  year: 2011
  ident: 10.14348/molcells.2023.0026_bib7
  article-title: Linear ubiquitination prevents inflammation and regulates immune signalling
  publication-title: Nature
  doi: 10.1038/nature09816
  contributor:
    fullname: Gerlach
– volume: 106
  start-page: 145
  year: 2001
  ident: 10.14348/molcells.2023.0026_bib11
  article-title: Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
  publication-title: Cell
  doi: 10.1016/S0092-8674(01)00434-2
  contributor:
    fullname: Katzmann
– volume: 19
  start-page: 254
  year: 2014
  ident: 10.14348/molcells.2023.0026_bib33
  article-title: Suppression of LUBAC‐mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN
  publication-title: Genes Cells
  doi: 10.1111/gtc.12128
  contributor:
    fullname: Takiuchi
– volume: 12
  start-page: 450
  year: 2020
  ident: 10.14348/molcells.2023.0026_bib5
  article-title: The multifaceted roles of the tumor susceptibility gene 101 (TSG101) in normal development and disease
  publication-title: Cancers (Basel)
  doi: 10.3390/cancers12020450
  contributor:
    fullname: Ferraiuolo
– volume: 100
  start-page: 7626
  year: 2003
  ident: 10.14348/molcells.2023.0026_bib22
  article-title: TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0932599100
  contributor:
    fullname: Lu
– volume: 136
  start-page: 1098
  year: 2009
  ident: 10.14348/molcells.2023.0026_bib26
  article-title: Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation
  publication-title: Cell
  doi: 10.1016/j.cell.2009.03.007
  contributor:
    fullname: Rahighi
– volume: 25
  start-page: 4877
  year: 2006
  ident: 10.14348/molcells.2023.0026_bib13
  article-title: A ubiquitin ligase complex assembles linear polyubiquitin chains
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601360
  contributor:
    fullname: Kirisako
– volume: 471
  start-page: 633
  year: 2011
  ident: 10.14348/molcells.2023.0026_bib34
  article-title: SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
  publication-title: Nature
  doi: 10.1038/nature09815
  contributor:
    fullname: Tokunaga
– volume: 63
  start-page: 990
  year: 2016
  ident: 10.14348/molcells.2023.0026_bib2
  article-title: SPATA2 links CYLD to LUBAC, activates CYLD, and controls LUBAC signaling
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2016.08.001
  contributor:
    fullname: Elliott
– volume: 3
  start-page: e03464
  year: 2014
  ident: 10.14348/molcells.2023.0026_bib27
  article-title: TNFR1-dependent cell death drives inflammation in Sharpin-deficient mice
  publication-title: Elife
  doi: 10.7554/eLife.03464
  contributor:
    fullname: Rickard
– volume: 54
  start-page: 335
  year: 2014
  ident: 10.14348/molcells.2023.0026_bib3
  article-title: Molecular basis and regulation of OTULIN-LUBAC interaction
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2014.03.018
  contributor:
    fullname: Elliott
– volume: 283
  start-page: 24295
  year: 2008
  ident: 10.14348/molcells.2023.0026_bib36
  article-title: c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor α (TNFα)-induced NF-κB activation
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C800128200
  contributor:
    fullname: Varfolomeev
– volume: 75
  start-page: 467
  year: 1997
  ident: 10.14348/molcells.2023.0026_bib24
  article-title: The breast cancer gene product TSG101: a regulator of ubiquitination?
  publication-title: J. Mol. Med. (Berl.)
  contributor:
    fullname: Ponting
– volume: 31
  start-page: 3833
  year: 2012
  ident: 10.14348/molcells.2023.0026_bib30
  article-title: The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING‐IBR‐RING domain and the unique LDD extension
  publication-title: EMBO J.
  doi: 10.1038/emboj.2012.217
  contributor:
    fullname: Smit
– volume: 35
  start-page: 1868
  year: 2016
  ident: 10.14348/molcells.2023.0026_bib38
  article-title: SPATA 2 links CYLD to the TNF‐α receptor signaling complex and modulates the receptor signaling outcomes
  publication-title: EMBO J.
  doi: 10.15252/embj.201694300
  contributor:
    fullname: Wagner
– volume: 16
  start-page: 2271
  year: 2016
  ident: 10.14348/molcells.2023.0026_bib15
  article-title: SPATA2-mediated binding of CYLD to HOIP enables CYLD recruitment to signaling complexes
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2016.07.086
  contributor:
    fullname: Kupka
– volume: 503
  start-page: 422
  year: 2013
  ident: 10.14348/molcells.2023.0026_bib32
  article-title: Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
  publication-title: Nature
  doi: 10.1038/nature12638
  contributor:
    fullname: Stieglitz
– volume: 60
  start-page: 1736
  year: 2000
  ident: 10.14348/molcells.2023.0026_bib4
  article-title: TSG101 protein steady-state level is regulated posttranslationally by an evolutionarily conserved COOH-terminal sequence
  publication-title: Cancer Res.
  contributor:
    fullname: Feng
– volume: 36
  start-page: 831
  year: 2009
  ident: 10.14348/molcells.2023.0026_bib8
  article-title: Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2009.10.013
  contributor:
    fullname: Haas
– volume: 9
  start-page: 153
  year: 2014
  ident: 10.14348/molcells.2023.0026_bib23
  article-title: HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.08.066
  contributor:
    fullname: Peltzer
– volume: 73
  start-page: 1138
  year: 2019
  ident: 10.14348/molcells.2023.0026_bib17
  article-title: MST1 negatively regulates TNFα-induced NF-κB signaling through modulating LUBAC activity
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.01.022
  contributor:
    fullname: Lee
– volume: 23
  start-page: 1192
  year: 2018
  ident: 10.14348/molcells.2023.0026_bib6
  article-title: Cooperative domain formation by homologous motifs in HOIL-1L and SHARPIN plays a crucial role in LUBAC stabilization
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2018.03.112
  contributor:
    fullname: Fujita
– volume: 529
  start-page: 546
  year: 2016
  ident: 10.14348/molcells.2023.0026_bib16
  article-title: Structure of a HOIP/E2~ ubiquitin complex reveals RBR E3 ligase mechanism and regulation
  publication-title: Nature
  doi: 10.1038/nature16511
  contributor:
    fullname: Lechtenberg
– volume: 153
  start-page: 1312
  year: 2013
  ident: 10.14348/molcells.2023.0026_bib12
  article-title: OTULIN antagonizes LUBAC signaling by specifically hydrolyzing Met1-linked polyubiquitin
  publication-title: Cell
  doi: 10.1016/j.cell.2013.05.014
  contributor:
    fullname: Keusekotten
– volume: 21
  start-page: 2397
  year: 2002
  ident: 10.14348/molcells.2023.0026_bib25
  article-title: Structure and functional interactions of the Tsg101 UEV domain
  publication-title: EMBO J.
  doi: 10.1093/emboj/21.10.2397
  contributor:
    fullname: Pornillos
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Snippet Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of...
SourceID pubmedcentral
crossref
pubmed
SourceType Open Access Repository
Aggregation Database
Index Database
StartPage 430
SubjectTerms Genes, Regulator
NF-kappa B
Signal Transduction
Tumor Necrosis Factor-alpha - pharmacology
Ubiquitins
Title TSG101 Physically Interacts with Linear Ubiquitin Chain Assembly Complex (LUBAC) and Upregulates the TNFα-Induced NF-κB Activation
URI https://www.ncbi.nlm.nih.gov/pubmed/37431163
https://pubmed.ncbi.nlm.nih.gov/PMC10336271
Volume 46
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