Arrangement of Annexin A2 tetramer and its impact on the structure and diffusivity of supported lipid bilayers

K. Fritz, G. Fritz, Barbara Windschiegl, C. Steinem, B. Nickel

    Research output: Contribution to journalJournal articleResearchpeer-review


    Annexins are a family of proteins that bind to anionic phospholipid membranes in a Ca2+-dependent manner. Annexin A2 forms heterotetramers (Anx A2t) with the S100A10 (p11) protein dimer. The tetramer is capable of bridging phospholipid membranes and it has been suggested to play a role in Ca2+-dependent exocytosis and cell-cell adhesion of metastatic cells. Here, we employ X-ray reflectivity measurements to resolve the conformation of Anx A2t upon Ca2+-dependent binding to single supported lipid bilayers (SLBs) composed of different mixtures of anionic (POPS) and neutral (POPC) phospholipids. Based on our results we propose that Anx A2t binds in a side-by-side configuration, i.e., both Anx A2 monomers bind to the bilayer with the p11 dimer positioned on top. Furthermore, we observe a strong decrease of lipid mobility upon binding of Anx A2t to SLBs with varying POPS content. X-Ray reflectivity measurements indicate that binding of Anx A2t also increases the density of the SLB. Interestingly, in the protein-facing leaflet of the SLB the lipid density is higher than in the substrate-facing leaflet. This asymmetric densification of the lipid bilayer by Anx A2t and Ca2+ might have important implications for the biochemical mechanism of Anx A2t-induced endo- and exocytosis.
    Original languageEnglish
    JournalSoft Matter
    Issue number17
    Pages (from-to)4084-4094
    Publication statusPublished - 2010


    Dive into the research topics of 'Arrangement of Annexin A2 tetramer and its impact on the structure and diffusivity of supported lipid bilayers'. Together they form a unique fingerprint.

    Cite this