Membrane protein sequestering by ionic protein–lipid interactions

Geert van den Bogaart, Karsten Meyenberg, H. Jelger Risselada, Hayder Amin, Katrin I. Willig, Barbara E. Hubrich, Markus Dier, Stefan W. Hell, Helmut Grubmüller, Ulf Diederichsen and Reinhard Jahn ()
Additional contact information
Geert van den Bogaart: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Karsten Meyenberg: Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2
H. Jelger Risselada: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Hayder Amin: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Katrin I. Willig: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Barbara E. Hubrich: Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2
Markus Dier: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Stefan W. Hell: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Helmut Grubmüller: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11
Ulf Diederichsen: Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2
Reinhard Jahn: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11

Nature, 2011, vol. 479, issue 7374, 552-555

Abstract: Electrostatic factors in membrane organization Exocytosis in neuronal cells requires the SNARE protein syntaxin-1A, which is clustered at sites where synaptic vesicles are poised to undergo exocytosis. Reinhard Jahn and colleagues use super-resolution stimulated-emission depletion (STED) microscopy to show that syntaxin clusters in the membrane through electrostatic interactions with the strongly anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2) into 70-nanometre microdomains. The results demonstrate that electrostatic protein–lipid interactions can result in the formation of microdomains independent of cholesterol or lipid phases and have important implications for the organization of the plasma membrane.

Date: 2011
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DOI: 10.1038/nature10545

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