Type I IFN is siloed in endosomes.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
28 07 2020
Historique:
pubmed: 16 7 2020
medline: 18 9 2020
entrez: 16 7 2020
Statut: ppublish

Résumé

Type I IFN (IFN-I) is thought to be rapidly internalized and degraded following binding to its receptor and initiation of signaling. However, many studies report the persistent effects mediated by IFN-I for days or even weeks, both ex vivo and in vivo. These long-lasting effects are attributed to downstream signaling molecules or induced effectors having a long half-life, particularly in specific cell types. Here, we describe a mechanism explaining the long-term effects of IFN-I. Following receptor binding, IFN-I is siloed into endosomal compartments. These intracellular "IFN silos" persist for days and can be visualized by fluorescence and electron microscopy. However, they are largely dormant functionally, due to IFN-I-induced negative regulators. By contrast, in individuals lacking these negative regulators, such as ISG15 or USP18, this siloed IFN-I can continue to signal from within the endosome. This mechanism may underlie the long-term effects of IFN-I therapy and may contribute to the pathophysiology of type I interferonopathies.

Identifiants

pubmed: 32665439
pii: 1921324117
doi: 10.1073/pnas.1921324117
pmc: PMC7395562
doi:

Substances chimiques

Cytokines 0
Interferon Type I 0
Ubiquitins 0
ISG15 protein, human 60267-61-0
USP18 protein, human EC 3.4.19.12
Ubiquitin Thiolesterase EC 3.4.19.12

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

17510-17512

Subventions

Organisme : NIA NIH HHS
ID : P30 AG008051
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI127372
Pays : United States
Organisme : NIAID NIH HHS
ID : T32 AI007647
Pays : United States

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Jennie B Altman (JB)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

Justin Taft (J)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

Tim Wedeking (T)

Division of Biophysics, Department of Biology, Osnabrück University, 49076 Osnabrück, Germany.

Conor N Gruber (CN)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

Michael Holtmannspötter (M)

Division of Biophysics, Department of Biology, Osnabrück University, 49076 Osnabrück, Germany.
Integrated Bioimaging Facility, Osnabrück University, 49076 Osnabrück, Germany.

Jacob Piehler (J)

Division of Biophysics, Department of Biology, Osnabrück University, 49076 Osnabrück, Germany.
Center for Cellular Nanoanalytics, Osnabrück University, 49076 Osnabrück, Germany.

Dusan Bogunovic (D)

Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029; dusan.bogunovic@mssm.edu.
Department of Pediatrics, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
Precision Immunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
Mindich Child Heath and Development Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029.

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Classifications MeSH