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Details on Person Many phosphorylations of RSV P protein at several serine and...
| Class:Id | Summation:9831529 |
|---|---|
| _displayName | Many phosphorylations of RSV P protein at several serine and... |
| _timestamp | 2023-07-10 08:38:15 |
| created | [InstanceEdit:9831548] Stephan, Ralf, 2023-03-22 |
| modified | [InstanceEdit:9832784] Stephan, Ralf, 2023-04-09 [InstanceEdit:9832787] Stephan, Ralf, 2023-04-09 [InstanceEdit:9838819] Orlic-Milacic, Marija, 2023-06-26 [InstanceEdit:9839741] Stephan, Ralf, 2023-07-10 |
| text | Many phosphorylations of RSV P protein at several serine and threonine residues are transient, with different turnover rates. This reaction tries to capture the temporarily phosphorylated P protein species, as these modifications appear to be essential in several processes. Dephosphorylated P protein, produced in bacteria, is unable to oligomerize. Transient phosphorylation at S116, S117 and S119 seems to be necessary for homotetramerization. Transient phosphorylation at T108 affects M2-1 transcriptional activities because this modification prevents interaction between the P and M2-1 proteins. In addition, P is phosphorylated and later dephosphorylated at S54 by a lithium-sensitive kinase regulating viral uncoating. Transient phosphorylation of S156 may play a role in the stability of the RdRp complex through oligomerization, P-L interaction, or P-RNP interaction (Navarro et al, 1991; Asenjo & Villanueva, 2000; Lu et al, 2002; Asenjo et al, 2006; Asenjo et al, 2008; Beavis et al, 2021). |
| (summation) | [BlackBoxEvent:9832782] p-S232-S237-P is further phosphorylated [Homo sapiens] |
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