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

Tutkimustuotosvertaisarvioitu

Standard

Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition. / Bilkova, Eva; Pleskot, Roman; Rissanen, Sami; Sun, Simou; Czogalla, Aleksander; Cwiklik, Lukasz; Róg, Tomasz; Vattulainen, Ilpo; Cremer, Paul S.; Jungwirth, Pavel; Coskun, Ünal.

julkaisussa: Journal of the American Chemical Society, Vuosikerta 139, Nro 11, 22.03.2017, s. 4019-4024.

Tutkimustuotosvertaisarvioitu

Harvard

Bilkova, E, Pleskot, R, Rissanen, S, Sun, S, Czogalla, A, Cwiklik, L, Róg, T, Vattulainen, I, Cremer, PS, Jungwirth, P & Coskun, Ü 2017, 'Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition', Journal of the American Chemical Society, Vuosikerta. 139, Nro 11, Sivut 4019-4024. https://doi.org/10.1021/jacs.6b11760

APA

Bilkova, E., Pleskot, R., Rissanen, S., Sun, S., Czogalla, A., Cwiklik, L., ... Coskun, Ü. (2017). Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition. Journal of the American Chemical Society, 139(11), 4019-4024. https://doi.org/10.1021/jacs.6b11760

Vancouver

Bilkova E, Pleskot R, Rissanen S, Sun S, Czogalla A, Cwiklik L et al. Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition. Journal of the American Chemical Society. 2017 maalis 22;139(11):4019-4024. https://doi.org/10.1021/jacs.6b11760

Author

Bilkova, Eva ; Pleskot, Roman ; Rissanen, Sami ; Sun, Simou ; Czogalla, Aleksander ; Cwiklik, Lukasz ; Róg, Tomasz ; Vattulainen, Ilpo ; Cremer, Paul S. ; Jungwirth, Pavel ; Coskun, Ünal. / Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition. Julkaisussa: Journal of the American Chemical Society. 2017 ; Vuosikerta 139, Nro 11. Sivut 4019-4024.

Bibtex - Lataa

@article{08194558904846bd8b7e0782c585eabd,
title = "Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition",
abstract = "The orchestrated recognition of phosphoinositides and concomitant intracellular release of Ca2+ is pivotal to almost every aspect of cellular processes, including membrane homeostasis, cell division and growth, vesicle trafficking, as well as secretion. Although Ca2+ 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 Ca2+ with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), the main lipid marker of the plasma membrane. Electrokinetic potential measurements of PI(4,5)P2 containing liposomes reveal that Ca2+ as well as Mg2+ reduce the zeta potential of liposomes to nearly background levels of pure phosphatidylcholine membranes. Strikingly, lipid recognition by the default PI(4,5)P2 lipid sensor, phospholipase C delta 1 pleckstrin homology domain (PLC δ1-PH), is completely inhibited in the presence of Ca2+, while Mg2+ 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 Ca2+ binding to the PI(4,5)P2 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)P2, 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.",
author = "Eva Bilkova and Roman Pleskot and Sami Rissanen and Simou Sun and Aleksander Czogalla and Lukasz Cwiklik and Tomasz R{\'o}g and Ilpo Vattulainen and Cremer, {Paul S.} and Pavel Jungwirth and {\"U}nal Coskun",
note = "EXT={"}Cwiklik, Lukasz{"}",
year = "2017",
month = "3",
day = "22",
doi = "10.1021/jacs.6b11760",
language = "English",
volume = "139",
pages = "4019--4024",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "11",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition

AU - Bilkova, Eva

AU - Pleskot, Roman

AU - Rissanen, Sami

AU - Sun, Simou

AU - Czogalla, Aleksander

AU - Cwiklik, Lukasz

AU - Róg, Tomasz

AU - Vattulainen, Ilpo

AU - Cremer, Paul S.

AU - Jungwirth, Pavel

AU - Coskun, Ünal

N1 - EXT="Cwiklik, Lukasz"

PY - 2017/3/22

Y1 - 2017/3/22

N2 - The orchestrated recognition of phosphoinositides and concomitant intracellular release of Ca2+ is pivotal to almost every aspect of cellular processes, including membrane homeostasis, cell division and growth, vesicle trafficking, as well as secretion. Although Ca2+ 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 Ca2+ with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), the main lipid marker of the plasma membrane. Electrokinetic potential measurements of PI(4,5)P2 containing liposomes reveal that Ca2+ as well as Mg2+ reduce the zeta potential of liposomes to nearly background levels of pure phosphatidylcholine membranes. Strikingly, lipid recognition by the default PI(4,5)P2 lipid sensor, phospholipase C delta 1 pleckstrin homology domain (PLC δ1-PH), is completely inhibited in the presence of Ca2+, while Mg2+ 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 Ca2+ binding to the PI(4,5)P2 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)P2, 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.

AB - The orchestrated recognition of phosphoinositides and concomitant intracellular release of Ca2+ is pivotal to almost every aspect of cellular processes, including membrane homeostasis, cell division and growth, vesicle trafficking, as well as secretion. Although Ca2+ 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 Ca2+ with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), the main lipid marker of the plasma membrane. Electrokinetic potential measurements of PI(4,5)P2 containing liposomes reveal that Ca2+ as well as Mg2+ reduce the zeta potential of liposomes to nearly background levels of pure phosphatidylcholine membranes. Strikingly, lipid recognition by the default PI(4,5)P2 lipid sensor, phospholipase C delta 1 pleckstrin homology domain (PLC δ1-PH), is completely inhibited in the presence of Ca2+, while Mg2+ 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 Ca2+ binding to the PI(4,5)P2 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)P2, 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.

U2 - 10.1021/jacs.6b11760

DO - 10.1021/jacs.6b11760

M3 - Article

VL - 139

SP - 4019

EP - 4024

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 11

ER -