| created | [InstanceEdit:9729799] Stephan, Ralf, 2021-05-03 |
| dbId | 9729789 |
| displayName | Signal recognition particle (SRP) triggers ribosome transloc... |
| modified | [InstanceEdit:9731332] Stephan, Ralf, 2021-05-19 |
| schemaClass | Summation |
| text |
Signal recognition particle (SRP) triggers ribosome translocation to the endoplasmic reticulum to ensure proper folding and trafficking of hydrophobic proteins to the cell membrane (Akopian et al, 2013). SARS-CoV-2 infection suppresses protein integration into the cell membrane. SARS-CoV-2 nonstructural protein 9 (nsp9) binds at a distinct and highly specific region in the S domain of the 7SL RNA scaffold of SRP, namely in the region that is bound by the SRP19 protein, which is required for proper folding and assembly of the SRP (including proper loading of SRP54), leading to suppression of protein integration into the cell membrane. This suggests that SARS-CoV-2-mediated suppression of SRP-dependent protein secretion enables suppression of host immune defenses (Banerjee et al, 2020). |
| (summation) |
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