Reactome | p-S232-S237-P is further phosphorylated

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

Locations in the PathwayBrowser

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Disease (Homo sapiens)

- Infectious disease (Homo sapiens)
  - Viral Infection Pathways (Homo sapiens)
    - Respiratory Syncytial Virus Infection Pathway (Homo sapiens)
      - Respiratory syncytial virus (RSV) genome replication, transcription and translation (Homo sapiens)
        
        Maturation of hRSV A proteins (Homo sapiens)
        
        p-S232-S237-P is further phosphorylated (Homo sapiens)

General

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SVG | | PPTX | SBGN

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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

PubMed ID	Title	Journal	Year
2045795	Location of phosphorylated residues in human respiratory syncytial virus phosphoprotein Villanueva, N, López-Otin, C, Navarro, J	J Gen Virol	1991
18706669	Phosphorylation of human respiratory syncytial virus P protein at serine 54 regulates viral uncoating González-Armas, JC, Asenjo, A, Villanueva, N	Virology	2008
10675554	Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization Villanueva, N, Asenjo, A	FEBS Lett	2000
34613802	Respiratory Syncytial Virus Phosphoprotein Residue S156 Plays a Role in Regulating Genome Transcription and Replication Phan, SI, He, B, Teng, MN, Tran, KC, Barrozo, ER, Beavis, AC	J Virol	2021
17098979	Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex Calvo, E, Asenjo, A, Villanueva, N	J Gen Virol	2006
12368320	The major phosphorylation sites of the respiratory syncytial virus phosphoprotein are dispensable for virus replication in vitro Jin, H, Ma, CH, Brazas, R, Lu, B	J Virol	2002

Participants

Input

p-S232,S237-P [cytosol] (Human respiratory syncytial virus A)

Output

p-P [cytosol] (Human respiratory syncytial virus A)

Participates

as an event of

Maturation of hRSV A proteins (Homo sapiens)

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

Name	Identifier	Synonyms
respiratory syncytial virus infectious disease	DOID:1273

Authored

Stephan, R (2023-04-06)

Reviewed

Bergeron, HC (2023-11-03)

Created

Stephan, R (2023-04-09)