Journal
NATURE NANOTECHNOLOGY
Volume 11, Issue 9, Pages 783-790Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NNANO.2016.89
Keywords
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Funding
- ANR [ANR-12-BS10-009-01, ANR-12-BSV8-0006-01]
- European Research Council (ERC) [310080]
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV8-0006] Funding Source: Agence Nationale de la Recherche (ANR)
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Annexins are abundant cytoplasmic proteins that can bind to negatively charged phospholipids in a Ca2+-dependent manner, and are known to play a role in the storage of Ca2+ and membrane healing. Little is known, however, about the dynamic processes of protein-Ca2+-membrane assembly and disassembly. Here we show that high-speed atomic force microscopy (HS-AFM) can be used to repeatedly induce and disrupt annexin assemblies and study their structure, dynamics and interactions. Our HS-AFM set-up is adapted for such biological applications through the integration of a pumping system for buffer exchange and a pulsed laser system for uncaging caged compounds. We find that biochemically identical annexins (annexin V) display different effective Ca2+ and membrane affinities depending on the assembly location, providing a wide Ca2+ buffering regime while maintaining membrane stabilization. We also show that annexin is membrane-recruited and forms stable supramolecular assemblies within 5 s in conditions that are comparable to a membrane lesion in a cell. Molecular dynamics simulations provide atomic detail of the role played by Ca2+ in the reversible binding of annexin to the membrane surface.
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