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Shimotai Y, Goto T, Matsuzaki Y, et al. The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing. Biochem Biophys Rep. 2015;3:1-6doi: 10.1016/j.bbrep.2015.07.001.
Shimotai, Y., Goto, T., Matsuzaki, Y., Muraki, Y., Sugawara, K., & Hongo, S. (2015). The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing. Biochemistry and biophysics reports, 31-6. https://doi.org/10.1016/j.bbrep.2015.07.001
Shimotai, Yoshitaka, et al. "The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing." Biochemistry and biophysics reports vol. 3 (2015): 1-6. doi: https://doi.org/10.1016/j.bbrep.2015.07.001
Shimotai Y, Goto T, Matsuzaki Y, Muraki Y, Sugawara K, Hongo S. The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing. Biochem Biophys Rep. 2015 Jul 08;3:1-6. doi: 10.1016/j.bbrep.2015.07.001. eCollection 2015 Sep. PMID: 29124162; PMCID: PMC5668659.
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Biochem Biophys Rep. 2015 Jul 08;3:1-6. doi: 10.1016/j.bbrep.2015.07.001. eCollection 2015 Sep.

The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing.

Biochemistry and biophysics reports

Yoshitaka Shimotai, Takanari Goto, Yoko Matsuzaki, Yasushi Muraki, Kanetsu Sugawara, Seiji Hongo

Affiliations

  1. Department of Infectious Diseases, Yamagata University Faculty of Medicine, 2-2-2 Iida-Nishi, Yamagata 990-9585, Japan.
  2. Department of Microbiology, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.

PMID: 29124162 PMCID: PMC5668659 DOI: 10.1016/j.bbrep.2015.07.001

Abstract

CM2 is an integral membrane protein encoded by the influenza C virus M gene. To examine the effects of the cytoplasmic tail of CM2 on its biochemical properties, deletion and substitution mutations were introduced into CM2 cytoplasmic tail at residues 47-115, and the expressed CM2 mutants were investigated. Although the cytoplasmic tail is not essential for the oligomerization of CM2, it may affect the degree of oligomerization. The residues 47-48, 67-69, 73-90 and 113-115 were all required for the proper expression of CM2. Pulse-chase experiments suggest that residues 47-48, 67-69, 73-75 and 79-87 stabilize CM2, thereby affecting CM2 expression. The C-terminal region at residues 61-115 is not essential for CM2 transport to the cell surface, and a 14-amino-acid, but not an 11-amino-acid, cytoplasmic tail is sufficient for the cell surface expression of CM2. These results suggest that either certain amino acid sequences or the length of the CM2 cytoplasmic tail are necessary for the proper conformational maturation, stability, expression level and intracellular transport of CM2.

Keywords: Biochemical property; CM2; Cytoplasmic tail; Influenza C virus; Ion channel

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