p-S232-S237-P is further phosphorylated

Stable Identifier
R-HSA-9832782
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
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p-S232-S237-P is further phosphorylated
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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).
Literature References
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Catalyst Activity

protein serine/threonine kinase activity of unknown kinase [cytosol]

Physical Entity
unknown kinase [cytosol] (Homo sapiens)
Activity
protein serine/threonine kinase activity (GO:0004674)
Disease
Cross References
Mondo
Authored
Stephan, R  (2023-04-06)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-04-09)
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