Cell autonomous inflammation in VEXAS is mediated by cGAS-STING
- bioRxiv. 2026 May 29:2026.05.26.727520. doi: 10.64898/2026.05.26.727520.
- 1. Center for Human Genetics and Genomics, NYU Grossman School of Medicine, New York, NY, USA.
- 2. Stem Cell Biochemistry Section, NIDCR, National Institutes of Health, Bethesda, MD, USA.
- 3. Institute for Systems Genetics, NYU Grossman School of Medicine, New York, NY, USA.
- 4. Division of Precision Medicine, Department of Medicine, NYU Grossman School of Medicine, New York, NY, USA.
- 5. Sorbonne Universite, Service de Medecine Interne, Hopital Saint Antoine, AP-HP, Paris, France.
- 6. Department of Pathology and Perlmutter Cancer Center, NYU Grossman School of Medicine, New York, NY, USA.
- 7. School of Clinical Medicine, University of Cambridge, Cambridge, UK.
- 8. Division of Hematology and Medical Oncology, Department of Medicine, Weill Cornell Medicine, New York, NY, USA.
- 9. New York Genome Center, New York, NY, USA.
- 10. Sandra and Edward Meyer Cancer Center, Weill Cornell Medicine, New York, NY, USA.
- 11. Mass Spectrometry Facility, NIDCR, National Institutes of Health, Bethesda, MD, USA.
- 12. NIDCR Imaging Core, NIDCR, National Institutes of Health, Bethesda, MD, USA.
- 13. Electron Microscopy Core, NHLBI, National Institutes of Health, Bethesda, MD, USA.
- 14. Department of Cell Biology, NYU Grossman School of Medicine, New York, NY, USA.
- 15. Department of Biomedical Engineering, NYU Tandon School of Engineering, Brooklyn, NY, USA.
- 16. Division of Rheumatology, Department of Medicine, NYU Grossman School of Medicine, New York, NY, USA.
- 17. Department of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, NY, USA.
VEXAS (vacuoles, E1 enzyme, X-linked, autoinflammatory, somatic) is a severe adult-onset inflammatory disease caused by somatic mutations that reduce cytoplasmic activity of UBA1, the primary initiating enzyme for ubiquitylation. How this hypomorphic state drives cell-intrinsic immune activation in mature myeloid cells is unknown. Using unbiased multi-omic, biochemical, and cell biological analyses of model systems and patient-derived cells, we show that loss of cytoplasmic UBA1 activity convergently disrupts endoplasmic reticulum-associated degradation (ERAD) and mitochondrial homeostasis. ERAD failure arises from preferential under-charging of ERAD E2 Enzymes, explaining hallmark VEXAS features, including ER-derived vacuoles and unfolded protein response activation, and promotes accumulation of the ERAD substrate STING. Simultaneously, mitochondrial dysfunction drives cytosolic leakage of mitochondrial DNA, inducing cGAS-dependent STING signaling and inflammatory cytokine production. STING inhibition or reversal of mitochondrial DNA leakage resolves multi-cytokine inflammation in VEXAS models and patient myeloid cells, establishing the cGAS-STING pathway as a therapeutically actionable vulnerability.
-
Cat. No.Product NameDescriptionTargetResearch Area
-
-
-
-
target: STINGResearch Areas: Inflammation/Immunology
-
-
Research Areas: Cancer
-
-
target: IRE1Research Areas: Metabolic Disease
-
target: ATF6
-
target: VDAC
-
target: STINGResearch Areas: Inflammation/Immunology
-
target: ApoptosisResearch Areas: Neurological Disease
-
-
Research Areas: Cancer
-
Research Areas: Cancer
-
target: E1/E2/E3 Enzyme