M2-1 tetramer gets phosphorylated

Stable Identifier
R-HSA-9832009
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
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M2-1 tetramer gets phosphorylated
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Phosphorylation of M2-1 occurs at S58 and S61 residues where there are consensus sequences for phosphorylation by casein kinase I (CK1). This process is essential for the antitermination activity of M2-1 (Lambert et al, 1988; Hardy & Wertz, 2000; Cartee & Wertz, 2001; Tang et al, 2001; Tanner et al, 2014).
Literature References
PubMed ID Title Journal Year
29489893 RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription

Eléouët, JF, Lassoued, S, Galloux, M, Richard, CA, Cardone, C, Rameix-Welti, MA, Sizun, C, Rincheval, V, Nekhai, S, Fix, J, Esneau, C

PLoS Pathog 2018
24434552 Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation

Trinh, CH, Kyle, HF, Carroll, MW, Barr, JN, Blondot, ML, Dods, RL, Hiscox, JA, Eléouët, JF, Trincão, J, Richard, CA, Wu, W, Tanner, SJ, Edwards, TA, Ariza, A, Silman, NJ

Proc Natl Acad Sci U S A 2014
10846068 The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is essential for protein function

Hardy, RW, Wertz, GW

J Virol 2000
11689613 Requirement of cysteines and length of the human respiratory syncytial virus M2-1 protein for protein function and virus viability

Nguyen, N, Tang, RS, Cheng, X, Jin, H

J Virol 2001
3339328 Kinetics of synthesis and phosphorylation of respiratory syncytial virus polypeptides

Lambert, DM, Diebold, M, Hambor, J, Galinski, B

J Gen Virol 1988
11711610 Respiratory syncytial virus M2-1 protein requires phosphorylation for efficient function and binds viral RNA during infection

Wertz, GW, Cartee, TL

J Virol 2001
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Authored
Stephan, R  (2023-03-24)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-03-28)
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