Dataset Information
Proteomic identification of MAVS carboxylation site–associated proteins
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: Tomohiko Okazaki
PROVIDER: PXD058403 | JPOST Repository | Wed Jul 23 00:00:00 BST 2025
REPOSITORIES: jPOST
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| 11a2683-6_33-6_5_TransitionResult.xlsx | Xlsx | |||
| 11a2683-6_33-6_5_TransitionResult_Summary.xlsx | Xlsx | |||
| MAVS_4A_11a2633.wiff | Wiff | |||
| MAVS_4A_11a2634.wiff | Wiff | |||
| MAVS_4A_11a2635.wiff | Wiff |
Items per page: 1 - 5 of 10 |
Publications
Membrane topology inversion of GGCX mediates cytoplasmic carboxylation for antiviral defense.
Science (New York, N.Y.) 20250703 6755
Mitochondrial antiviral signaling protein (MAVS) is an adaptor involved in antiviral immunity, but its regulation is not fully understood. We identified carboxylation of MAVS by vitamin K (VK)-dependent γ-glutamyl carboxylase (GGCX), which was unexpected owing to the reported membrane topology of GGCX. We found that GGCX could undergo topology inversion to carboxylate MAVS within the cytoplasm. This carboxylation enhanced the ability of MAVS to induce type I interferons while suppressing the ind ...[more]
