Evidence map›Paper›PMID 38789573›Full record

ArticleCell death and differentiation2024

EGFR inhibits TNF-α-mediated pathway by phosphorylating TNFR1 at tyrosine 360 and 401.

Young Woo Nam, June-Ha Shin, Seongmi Kim, Chi Hyun Hwang, Choong-Sil Lee, Gyuho Hwang, Hwa-Ryeon Kim, Jae-Seok Roe, Jaewhan Song

Erratum issuedAbstract read
In one paragraph

Article in Cell death and differentiation, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Young Woo NamDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.ORCID 0009-0008-1576-1749
June-Ha ShinDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.ORCID 0000-0002-6076-0090
Seongmi KimDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Chi Hyun HwangDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Choong-Sil LeeDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Gyuho HwangDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Hwa-Ryeon KimDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Jae-Seok RoeDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea.
Jaewhan SongDepartment of Biochemistry, College of Life Science and Technology, Institute for Bio-medical Convergence Science and Technology, Yonsei University, Seoul, Republic of Korea. jso678@yonsei.ac.kr.ORCID 0000-0001-8152-9210

Funding

Ministry of Science, ICT and Future Planning (MSIP) 2015R1A3A20665Ministry of Science, ICT and Future Planning (MSIP) 2015R1A3A2066581National Research Foundation of Korea (NRF) 2020R1A5A1019023
6 · The paper itself

Abstract

Tumour necrosis factor receptor 1 (TNFR1) induces the nuclear factor kappa-B (NF-κB) signalling pathway and regulated cell death processes when TNF-α ligates with it. Although mechanisms regulating the downstream pathways of TNFR1 have been elucidated, the direct regulation of TNFR1 itself is not well known. In this study, we showed that the kinase domain of the epidermal growth factor receptor (EGFR) regulates NF-κB signalling and TNF-α-induced cell death by directly phosphorylating TNFR1 at Tyr 360 and 401 in its death domain. In contrast, EGFR inhibition by EGFR inhibitors, such as erlotinib and gefitinib, prevented their interaction. Once TNFR1 is phosphorylated, its death domain induces the suppression of the NF-κB pathways, complex II-mediated apoptosis, or necrosome-dependent necroptosis. Physiologically, in mouse models, EGF treatment mitigates TNF-α-dependent necroptotic skin inflammation induced by treatment with IAP and caspase inhibitors. Our study revealed a novel role for EGFR in directly regulating TNF-α-related pathways.

Indexed as

ErbB ReceptorsReceptors, Tumor Necrosis Factor, Type ISignal TransductionTumor Necrosis Factor-alphaAnimalsApoptosisErlotinib HydrochlorideGefitinibHumansMiceMice, Inbred C57BLNF-kappa BPhosphorylationTyrosineEGFR protein, humanErbB ReceptorsErlotinib HydrochlorideGefitinibNF-kappa BReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alphaTyrosine

Identifiers

PMID38789573
PMCPMC11445491

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.