Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length

Sandra Schick, Lirong Chen, Edwin Li, Janice Lin, Ingo Koper, Kalina Hristova

    Research output: Contribution to journalArticlepeer-review

    26 Citations (Scopus)


    The influenza virus matrix protein 2 (M2) assembles into a tetramer in the host membrane during viral uncoating and maturation. It has been used as a model system to understand the relative contributions of protein-lipid and protein-protein interactions to membrane protein structure and association. Here we investigate the effect of lipid chain length on the association of the M2 transmembrane domain into tetramers using Forster resonance energy transfer. We observe that the interactions between the M2 helices are much stronger in 1,2-dilauroyl-sn-glycero-3-phosphocholine than in 1-palmitoyl-2-oleoyl-sn-glyc- ero-3-phosphocholine bilayers. Thus, lipid chain length and bilayer thickness not only modulate peptide interactions, but could also be a major determinant of the association of transmembrane helices into functional membrane protein oligomers.

    Original languageEnglish
    Pages (from-to)1810-1817
    Number of pages8
    JournalBiophysical Journal
    Issue number6
    Publication statusPublished - 2010


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