Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition.

Eva Bilkova, Roman Pleskot, Sami Rissanen, Simou Sun, Aleksander Czogalla, Lukasz Cwiklik, Tomasz Róg, Ilpo Vattulainen, Paul S Cremer, Pavel Jungwirth, Ünal Coskun

Journal: Journal of the American Chemical Society 2018;139(11):4019-4024

PMID: 28177616

Abstract

The orchestrated recognition of phosphoinositides and concomitant intracellular release of Ca is pivotal to almost every aspect of cellular processes, including membrane homeostasis, cell division and growth, vesicle trafficking, as well as secretion. Although Ca is known to directly impact phosphoinositide clustering, little is known about the molecular basis for this or its significance in cellular signaling. Here, we study the direct interaction of Ca with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P), the main lipid marker of the plasma membrane. Electrokinetic potential measurements of PI(4,5)P containing liposomes reveal that Ca as well as Mg reduce the zeta potential of liposomes to nearly background levels of pure phosphatidylcholine membranes. Strikingly, lipid recognition by the default PI(4,5)P lipid sensor, phospholipase C delta 1 pleckstrin homology domain (PLC δ1-PH), is completely inhibited in the presence of Ca, while Mg has no effect with 100 nm liposomes and modest effect with giant unilamellar vesicles. Consistent with biochemical data, vibrational sum frequency spectroscopy and atomistic molecular dynamics simulations reveal how Ca binding to the PI(4,5)P headgroup and carbonyl regions leads to confined lipid headgroup tilting and conformational rearrangements. We rationalize these findings by the ability of calcium to block a highly specific interaction between PLC δ1-PH and PI(4,5)P, encoded within the conformational properties of the lipid itself. Our studies demonstrate the possibility that switchable phosphoinositide conformational states can serve as lipid recognition and controlled cell signaling mechanisms.

Address: Paul Langerhans Institute Dresden of the Helmholtz Zentrum München at the University Hospital and Faculty of Medicine Carl Gustav Carus of TU Dresden, Technische Universität Dresden , Fetscher Strasse 74, 01307 Dresden, Germany.; German Center for Diabetes Research (DZD e.V.) , Ingolstädter Landstraße 1, 85764 Neuherberg, Germany.; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic , Flemingovo náměstí 2, 16610 Prague 6, Czech Republic.; Institute of Experimental Botany, Academy of Sciences of the Czech Republic , v.v.i., Rozvojová 263, 16502 Prague 6, Czech Republic.; Department of Physics, Tampere University of Technology , P.O. Box 692, FI-33101 Tampere, Finland.; Laboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław , Joliot-Curie 14a, 50-383 Wrocław, Poland.; J. Heyrovský Institute of Physical Chemistry, Academy of Sciences of the Czech Republic , v.v.i., Dolejskova 3, 18223 Prague 8, Czech Republic.; Department of Physics, University of Helsinki , P.O. Box 64, FI-00014, Helsinki, Finland.; MEMPHYS- Center for Biomembrane Physics, University of Southern Denmark , DK-5230 Odense, Denmark.
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