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Details on Person In resting cells, myxovirus resistance protein 2 (MX2, also ...
| Class:Id | Summation:9962626 |
|---|---|
| _displayName | In resting cells, myxovirus resistance protein 2 (MX2, also ... |
| _timestamp | 2025-08-08 17:45:05 |
| created | [InstanceEdit:9962691] Shamovsky, Veronica, 2025-08-08 |
| literatureReference | [LiteratureReference:9962661] MX2 Viral Substrate Breadth and Inhibitory Activity Are Regulated by Protein Phosphorylation [LiteratureReference:9962721] MX2-mediated innate immunity against HIV-1 is regulated by serine phosphorylation [LiteratureReference:9962610] The GTPase Domain of MX2 Interacts with the HIV-1 Capsid, Enabling Its Short Isoform to Moderate Antiviral Restriction [LiteratureReference:9962652] MxB Restricts HIV-1 by Targeting the Tri-hexamer Interface of the Viral Capsid [LiteratureReference:9962599] Multiple components of the nuclear pore complex interact with the amino-terminus of MX2 to facilitate HIV-1 restriction |
| text | In resting cells, myxovirus resistance protein 2 (MX2, also known as MxB) is phosphorylated at serine residues 14, 17, and 18 within its N-terminal domain by unidentified cellular kinases. These residues lie within a region critical for nuclear envelope localization and viral capsid recognition (Dicks MDJ et al. 2018; Betancor G et al., 2019; Smaga SS et al., 2019). Phosphorylation at these sites suppresses the antiviral activity of MX2 by preventing its interaction with the viral capsid and nuclear transport factors. Dephosphorylation of these serines, catalyzed by the myosin light chain phosphatase (MLCP) complex, specifically its protein phosphatase 1 catalytic subunit-β (PPP1CB), restores MX2’s full antiviral function (Betancor G et al., 2021, 2022). |
| (summation) | [Reaction:9962583] MX2 is phosphorylated at S14, S17, S18 [Homo sapiens] |
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No pathways have been reviewed or authored by In resting cells, myxovirus resistance protein 2 (MX2, also ... (9962626)
