M dimer is phosphorylated

Stable Identifier
R-HSA-9831712
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
nucleoplasm
ReviewStatus
5/5
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M dimer is phosphorylated
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Phosphorylation of RSV matrix protein M in the nucleus is necessary for M oligomerization and export to cytosol as well as its later retention in cytosol. Modification takes place at S95 and T205 and is catalyzed by cellular casein kinase II (CKII, CK2) (Bajorek et al, 2014; Ghildyal et al, 2022).
Literature References
PubMed ID Title Journal Year
35887322 Nuclear Transport of Respiratory Syncytial Virus Matrix Protein Is Regulated by Dual Phosphorylation Sites

Ghildyal, R, Teng, MN, Tran, KC, Mills, J, Casarotto, MG, Bardin, PG, Jans, DA

Int J Mol Sci 2022
24672034 The Thr205 phosphorylation site within respiratory syncytial virus matrix (M) protein modulates M oligomerization and virus production

Bajorek, M, Caly, L, Tran, KC, Maertens, GN, Tripp, RA, Bacharach, E, Teng, MN, Ghildyal, R, Jans, DA

J Virol 2014
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein serine/threonine kinase activity of Casein kinase II [nucleoplasm]

Physical Entity
Casein kinase II [nucleoplasm] (Homo sapiens)
Activity
protein serine/threonine kinase activity (GO:0004674)
Disease
Cross References
Mondo
Authored
Stephan, R  (2023-03-22)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-03-24)
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