Evidence map›Paper›PMID 32926474›Full record

ArticleThe EMBO journal2020

EGFR-mediated tyrosine phosphorylation of STING determines its trafficking route and cellular innate immunity functions.

Chenyao Wang, Xin Wang, Manoj Veleeparambil, Patricia M Kessler, Belinda Willard, Saurabh Chattopadhyay, Ganes C Sen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
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

47 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  5. Lactylation: a novel post-translational modification for cGAS-STING pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
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  19. The STING signaling pathways and bacterial infection.Apoptosis : an international journal on programmed cell death · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Chenyao WangDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
Xin WangDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
Manoj VeleeparambilDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.ORCID 0000-0003-3545-5251
Patricia M KesslerDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
Belinda WillardDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
Saurabh ChattopadhyayDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.
Ganes C SenDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA.ORCID 0000-0002-9692-0631
Cleveland Clinic Lerner College of Medicine · US

Funding

TELOMERASE INACTIVATION BY RNASE L SIGNALS CELL DEATHP01CA062220 · NCI · CLEVELAND CLINIC LERNER COM-CWRU · PI LI, XIAOXIA, STARK, GEORGE ROBERT · 1994 to 2020
$35.6M
ANTIVIRAL ACTIONS OF INTERFERONSR01CA068782 · NCI · CLEVELAND CLINIC LERNER COM-CWRU · PI SEN, GANES C. · 1995 to 2020
$7.6M
High-End Instrumentation (HEI) Grant Program (S10)S10OD023436 · OD · CLEVELAND CLINIC LERNER COM-CWRU · PI WILLARD, BELINDA BELLE · 2017 to 2017
$873k
HHS | National Institutes of Health (NIH) 1S10OD023436-01HHS | NIH | National Cancer Institute (NCI) CA062220HHS | NIH | National Cancer Institute (NCI) CA068782NCI NIH HHS P01 CA062220NCI NIH HHS R01 CA068782NIH HHS S10 OD023436
6 · The paper itself

Abstract

STING (STimulator of INterferon Genes) mediates protective cellular response to microbial infection and tissue damage, but its aberrant activation can lead to autoinflammatory diseases. Upon ligand stimulation, the endoplasmic reticulum (ER) protein STING translocates to endosomes for induction of interferon production, while an alternate trafficking route delivers it directly to the autophagosomes. Here, we report that phosphorylation of a specific tyrosine residue in STING by the epidermal growth factor receptor (EGFR) is required for directing STING to endosomes, where it interacts with its downstream effector IRF3. In the absence of EGFR-mediated phosphorylation, STING rapidly transits into autophagosomes, and IRF3 activation, interferon production, and antiviral activity are compromised in cell cultures and mice, while autophagic activity is enhanced. Our observations illuminate a new connection between the tyrosine kinase activity of EGFR and innate immune functions of STING and suggest new experimental and therapeutic approaches for selective regulation of STING functions.

Indexed as

Immunity, InnateAnimalsCell LineEndoplasmic ReticulumEndosomesErbB ReceptorsGene Knockdown TechniquesHeLa CellsHumansInterferon Regulatory Factor-3MaleMembrane ProteinsMiceMice, Inbred C57BLPhosphorylationProtein TransportEGFR protein, humanEGFR protein, mouseErbB ReceptorsInterferon Regulatory Factor-3IRF3 protein, humanIrf3 protein, mouseMembrane ProteinsSTING1 protein, humanSting1 protein, mouseSTING ProteinTyrosineEGFRendosomesIRF3STING signalingtyrosine phosphorylation

Identifiers

PMID32926474
PMCPMC7667877
OpenAlexW3085186302

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.