TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1

Jianwen Zhou; Nikoline Lander Rasmussen; Hallvard Lauritz Olsvik; Vyacheslav Akimov; Zehan Hu; Gry Evjen; Stéphanie Kaeser-Pebernard; Devanarayanan Siva Sankar; Carole Roubaty; Pauline Verlhac; Nicole van de Beck; Fulvio Reggiori; Yakubu Princely Abudu; Blagoy Blagoev; Trond Lamark; Terje Johansen; Jörn Dengjel

doi:10.1083/jcb.202108144

TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1

Jianwen Zhou, Nikoline Lander Rasmussen, Hallvard Lauritz Olsvik, Vyacheslav Akimov, Zehan Hu, Gry Evjen, Stéphanie Kaeser-Pebernard, Devanarayanan Siva Sankar, Carole Roubaty, Pauline Verlhac, Nicole van de Beck, Fulvio Reggiori, Yakubu Princely Abudu, Blagoy Blagoev, Trond Lamark, Terje Johansen, Jörn Dengjel

Institut for Biomedicin - Forskning og uddannelse, Vest

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

11 Citationer (Scopus)

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Abstract

Limitation of excessive inflammation due to selective degradation of pro-inflammatory proteins is one of the cytoprotective functions attributed to autophagy. In the current study, we highlight that selective autophagy also plays a vital role in promoting the establishment of a robust inflammatory response. Under inflammatory conditions, here TLR3-activation by poly(I:C) treatment, the inflammation repressor TNIP1 (TNFAIP3 interacting protein 1) is phosphorylated by Tank-binding kinase 1 (TBK1) activating an LIR motif that leads to the selective autophagy-dependent degradation of TNIP1, supporting the expression of pro-inflammatory genes and proteins. This selective autophagy efficiently reduces TNIP1 protein levels early (0-4 h) upon poly(I:C) treatment to allow efficient initiation of the inflammatory response. At 6 h, TNIP1 levels are restored due to increased transcription avoiding sustained inflammation. Thus, similarly as in cancer, autophagy may play a dual role in controlling inflammation depending on the exact state and timing of the inflammatory response.

Originalsprog	Engelsk
Artikelnummer	e202108144
Tidsskrift	The Journal of Cell Biology
Vol/bind	222
Nummer	2
Antal sider	28
ISSN	0021-9525
DOI	https://doi.org/10.1083/jcb.202108144
Status	Udgivet - feb. 2023

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10.1083/jcb.202108144Licens: CC BY-NC-SA

jcb_202108144Forlagets udgivne version, 6,95 MBLicens: CC BY-NC-SA

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Zhou, J., Rasmussen, N. L., Olsvik, H. L., Akimov, V., Hu, Z., Evjen, G., Kaeser-Pebernard, S., Sankar, D. S., Roubaty, C., Verlhac, P., van de Beck, N., Reggiori, F., Abudu, Y. P., Blagoev, B., Lamark, T., Johansen, T., & Dengjel, J. (2023). TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1. The Journal of Cell Biology, 222(2), Artikel e202108144. https://doi.org/10.1083/jcb.202108144

@article{eb658081c42c4782bb7cc9c2a3a1dd66,

title = "TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1",

abstract = "Limitation of excessive inflammation due to selective degradation of pro-inflammatory proteins is one of the cytoprotective functions attributed to autophagy. In the current study, we highlight that selective autophagy also plays a vital role in promoting the establishment of a robust inflammatory response. Under inflammatory conditions, here TLR3-activation by poly(I:C) treatment, the inflammation repressor TNIP1 (TNFAIP3 interacting protein 1) is phosphorylated by Tank-binding kinase 1 (TBK1) activating an LIR motif that leads to the selective autophagy-dependent degradation of TNIP1, supporting the expression of pro-inflammatory genes and proteins. This selective autophagy efficiently reduces TNIP1 protein levels early (0-4 h) upon poly(I:C) treatment to allow efficient initiation of the inflammatory response. At 6 h, TNIP1 levels are restored due to increased transcription avoiding sustained inflammation. Thus, similarly as in cancer, autophagy may play a dual role in controlling inflammation depending on the exact state and timing of the inflammatory response.",

author = "Jianwen Zhou and Rasmussen, {Nikoline Lander} and Olsvik, {Hallvard Lauritz} and Vyacheslav Akimov and Zehan Hu and Gry Evjen and St{\'e}phanie Kaeser-Pebernard and Sankar, {Devanarayanan Siva} and Carole Roubaty and Pauline Verlhac and {van de Beck}, Nicole and Fulvio Reggiori and Abudu, {Yakubu Princely} and Blagoy Blagoev and Trond Lamark and Terje Johansen and J{\"o}rn Dengjel",

note = "{\textcopyright} 2022 Zhou et al.",

year = "2023",

month = feb,

doi = "10.1083/jcb.202108144",

language = "English",

volume = "222",

journal = "The Journal of Cell Biology",

issn = "0021-9525",

publisher = "Rockefeller University Press",

number = "2",

}

Zhou, J, Rasmussen, NL, Olsvik, HL, Akimov, V, Hu, Z, Evjen, G, Kaeser-Pebernard, S, Sankar, DS, Roubaty, C, Verlhac, P, van de Beck, N, Reggiori, F, Abudu, YP, Blagoev, B, Lamark, T, Johansen, T & Dengjel, J 2023, 'TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1', The Journal of Cell Biology, bind 222, nr. 2, e202108144. https://doi.org/10.1083/jcb.202108144

TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1. / Zhou, Jianwen; Rasmussen, Nikoline Lander; Olsvik, Hallvard Lauritz et al.
I: The Journal of Cell Biology, Bind 222, Nr. 2, e202108144, 02.2023.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

TY - JOUR

T1 - TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1

AU - Zhou, Jianwen

AU - Rasmussen, Nikoline Lander

AU - Olsvik, Hallvard Lauritz

AU - Akimov, Vyacheslav

AU - Hu, Zehan

AU - Evjen, Gry

AU - Kaeser-Pebernard, Stéphanie

AU - Sankar, Devanarayanan Siva

AU - Roubaty, Carole

AU - Verlhac, Pauline

AU - van de Beck, Nicole

AU - Reggiori, Fulvio

AU - Abudu, Yakubu Princely

AU - Blagoev, Blagoy

AU - Lamark, Trond

AU - Johansen, Terje

AU - Dengjel, Jörn

PY - 2023/2

Y1 - 2023/2

N2 - Limitation of excessive inflammation due to selective degradation of pro-inflammatory proteins is one of the cytoprotective functions attributed to autophagy. In the current study, we highlight that selective autophagy also plays a vital role in promoting the establishment of a robust inflammatory response. Under inflammatory conditions, here TLR3-activation by poly(I:C) treatment, the inflammation repressor TNIP1 (TNFAIP3 interacting protein 1) is phosphorylated by Tank-binding kinase 1 (TBK1) activating an LIR motif that leads to the selective autophagy-dependent degradation of TNIP1, supporting the expression of pro-inflammatory genes and proteins. This selective autophagy efficiently reduces TNIP1 protein levels early (0-4 h) upon poly(I:C) treatment to allow efficient initiation of the inflammatory response. At 6 h, TNIP1 levels are restored due to increased transcription avoiding sustained inflammation. Thus, similarly as in cancer, autophagy may play a dual role in controlling inflammation depending on the exact state and timing of the inflammatory response.

AB - Limitation of excessive inflammation due to selective degradation of pro-inflammatory proteins is one of the cytoprotective functions attributed to autophagy. In the current study, we highlight that selective autophagy also plays a vital role in promoting the establishment of a robust inflammatory response. Under inflammatory conditions, here TLR3-activation by poly(I:C) treatment, the inflammation repressor TNIP1 (TNFAIP3 interacting protein 1) is phosphorylated by Tank-binding kinase 1 (TBK1) activating an LIR motif that leads to the selective autophagy-dependent degradation of TNIP1, supporting the expression of pro-inflammatory genes and proteins. This selective autophagy efficiently reduces TNIP1 protein levels early (0-4 h) upon poly(I:C) treatment to allow efficient initiation of the inflammatory response. At 6 h, TNIP1 levels are restored due to increased transcription avoiding sustained inflammation. Thus, similarly as in cancer, autophagy may play a dual role in controlling inflammation depending on the exact state and timing of the inflammatory response.

U2 - 10.1083/jcb.202108144

DO - 10.1083/jcb.202108144

M3 - Journal article

C2 - 36574265

SN - 0021-9525

VL - 222

JO - The Journal of Cell Biology

JF - The Journal of Cell Biology

IS - 2

M1 - e202108144

ER -

TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1

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