M forms a homodimer

Stable Identifier
R-HSA-9831714
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
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M forms a homodimer
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Protein M dimerizes (Bajorek et al. 2014; Förster et al. 2015; Trevisan et al. 2018). M dimerization does not depend on its phosphorylation status suggesting that it happens spontaneously (Bajorek et al. 2014; Trevisan et al. 2018). A potassium ion may be involved in dimer stabilization (Förster et al. 2015).
Literature References
PubMed ID Title Journal Year
29510513 Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells

Alvisi, G, Radeghieri, A, Ghildyal, R, Di Antonio, V, Trevisan, M, Palù, G

Viruses 2018
25673702 Dimerization of matrix protein is required for budding of respiratory syncytial virus

Maertens, GN, Förster, A, Bajorek, M, Farrell, PJ

J Virol 2015
24672034 The Thr205 phosphorylation site within respiratory syncytial virus matrix (M) protein modulates M oligomerization and virus production

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

J Virol 2014
Participants
Input
Output
Participates
as an event of
Disease
Authored
Stephan, R  (2023-03-22)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-03-24)
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