Počet záznamů: 1
Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition
- 1.
SYSNO ASEP 0475201 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition Tvůrce(i) Bilkova, E. (DE)
Pleskot, Roman (UEB-Q) RID, ORCID
Rissanen, S. (FI)
Sun, S. (US)
Czogalla, A. (DE)
Cwiklik, Lukasz (UFCH-W) RID, ORCID
Róg, T. (FI)
Vattulainen, I. (FI)
Cremer, P. S. (US)
Jungwirth, P. (CZ)
Coskun, U. (DE)Celkový počet autorů 11 Zdroj.dok. Journal of the American Chemical Society. - : American Chemical Society - ISSN 0002-7863
Roč. 139, č. 11 (2017), s. 4019-4024Poč.str. 6 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova membrane ; calcium ions ; PIP2 ; molecular dynamics Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Cell biology Vědní obor RIV – spolupráce Ústav fyzikální chemie J.Heyrovského - Fyzikální chemie a teoretická chemie CEP GA13-19073S GA ČR - Grantová agentura ČR Institucionální podpora UEB-Q - RVO:61389030 ; UFCH-W - RVO:61388955 UT WOS 000397477700019 DOI 10.1021/jacs.6b11760 Anotace 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 sphosphate (PI(4,5)P-2), the main lipid marker of the plasma membrane. Electrokinetic potential measurements of PI(4,5)P-2 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)P-2 lipid sensor, phospholipase C delta 1 pleckstrin homology domain (PLC delta 1-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)P-2 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 delta 1-PH and PI(4,5)P-2, 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. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2018
Počet záznamů: 1