S trimers are recruited to the assembling virion through interaction with M protein (reviewed in Ujike and Taguchi, 2015). Multiple regions of M contribute to the recruitment of S, with a single tyrosine residue in the C-terminal domain of M playing a critical role (McBride et al, 2010a; Hsieh et al, 2008). Interaction with M is aided by a dibasic motif in the C-terminus of S, which promotes retrieval of the spike protein from the cell surface by binding the COPI coat (McBride et al, 2007; Ujike et al, 2016). Palmitoylation of the C-terminus of S appears dispensible for the interaction with M in SARS-COV-1, unlike the case in other coronaviruses (Ujike et al, 2012; McBride 2010b; reviewed in Ujike and Taguchi, 2015). Size estimates and modelling suggest the mature virion has approximately 300 S trimers (Neuman et al, 2006; reviewed in Chang et al, 2014).
Li, J, Machamer, CE, McBride, CE
Machamer, CE, McBride, CE
Ujike, M, Huang, C, Makino, S, Matsuyama, S, Shirato, K, Taguchi, F
Ujike, M, Taguchi, F
Ujike, M, Huang, C, Makino, S, Shirato, K, Taguchi, F
Chen, SC, Li, HC, Lo, SY, Hsieh, YC
Neuman, BW, Buchmeier, MJ, Milligan, RA, Yeager, M, Adair, BD, Orca, G, Kuhn, P, Yoshioka, C, Quispe, JD
Chang, CK, Hsiao, CD, Hou, MH, Chang, CF, Huang, TH
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