ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites

Ilya Bezprozvanny, Barbara E. Ehrlich

Research output: Contribution to journalArticle

137 Citations (Scopus)

Abstract

The inositol 1,4,5-trisphosphate (IP3) receptor, a Ca2+permeable channel, plays a key role in intracellular Ca2+ signaling. The effects of ATP on the IP3 receptor at the single-channel level were characterized after channel incorporation into planar lipid bilayers. ATP alone was not sufficient to open the IP3-gated channel, but addition of ATP or nonhydrolyzable ATP analogs in the presence of IP3 increased the frequency of channel openings 4.8-fold and increased the average duration of channel openings 2.5-fold; channel conductance was unchanged. High concentrations of ATP (>4 mM) decreased channel activity most probably by competing with IP3 for the IP3-binding site. Allosteric modulation of IP3-induced Ca2+ release by ATP may contribute to the maintenance of cell viability during periods of energy starvation.

Original languageEnglish (US)
Pages (from-to)1175-1184
Number of pages10
JournalNeuron
Volume10
Issue number6
DOIs
StatePublished - 1993

Fingerprint

Inositol 1,4,5-Trisphosphate
Adenosine Triphosphate
Inositol 1,4,5-Trisphosphate Receptors
Lipid Bilayers
Starvation
Cell Survival
Binding Sites
Maintenance

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites. / Bezprozvanny, Ilya; Ehrlich, Barbara E.

In: Neuron, Vol. 10, No. 6, 1993, p. 1175-1184.

Research output: Contribution to journalArticle

@article{ca25334396514856bd44539c016b1fc3,
title = "ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites",
abstract = "The inositol 1,4,5-trisphosphate (IP3) receptor, a Ca2+permeable channel, plays a key role in intracellular Ca2+ signaling. The effects of ATP on the IP3 receptor at the single-channel level were characterized after channel incorporation into planar lipid bilayers. ATP alone was not sufficient to open the IP3-gated channel, but addition of ATP or nonhydrolyzable ATP analogs in the presence of IP3 increased the frequency of channel openings 4.8-fold and increased the average duration of channel openings 2.5-fold; channel conductance was unchanged. High concentrations of ATP (>4 mM) decreased channel activity most probably by competing with IP3 for the IP3-binding site. Allosteric modulation of IP3-induced Ca2+ release by ATP may contribute to the maintenance of cell viability during periods of energy starvation.",
author = "Ilya Bezprozvanny and Ehrlich, {Barbara E.}",
year = "1993",
doi = "10.1016/0896-6273(93)90065-Y",
language = "English (US)",
volume = "10",
pages = "1175--1184",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "6",

}

TY - JOUR

T1 - ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites

AU - Bezprozvanny, Ilya

AU - Ehrlich, Barbara E.

PY - 1993

Y1 - 1993

N2 - The inositol 1,4,5-trisphosphate (IP3) receptor, a Ca2+permeable channel, plays a key role in intracellular Ca2+ signaling. The effects of ATP on the IP3 receptor at the single-channel level were characterized after channel incorporation into planar lipid bilayers. ATP alone was not sufficient to open the IP3-gated channel, but addition of ATP or nonhydrolyzable ATP analogs in the presence of IP3 increased the frequency of channel openings 4.8-fold and increased the average duration of channel openings 2.5-fold; channel conductance was unchanged. High concentrations of ATP (>4 mM) decreased channel activity most probably by competing with IP3 for the IP3-binding site. Allosteric modulation of IP3-induced Ca2+ release by ATP may contribute to the maintenance of cell viability during periods of energy starvation.

AB - The inositol 1,4,5-trisphosphate (IP3) receptor, a Ca2+permeable channel, plays a key role in intracellular Ca2+ signaling. The effects of ATP on the IP3 receptor at the single-channel level were characterized after channel incorporation into planar lipid bilayers. ATP alone was not sufficient to open the IP3-gated channel, but addition of ATP or nonhydrolyzable ATP analogs in the presence of IP3 increased the frequency of channel openings 4.8-fold and increased the average duration of channel openings 2.5-fold; channel conductance was unchanged. High concentrations of ATP (>4 mM) decreased channel activity most probably by competing with IP3 for the IP3-binding site. Allosteric modulation of IP3-induced Ca2+ release by ATP may contribute to the maintenance of cell viability during periods of energy starvation.

UR - http://www.scopus.com/inward/record.url?scp=0027210625&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027210625&partnerID=8YFLogxK

U2 - 10.1016/0896-6273(93)90065-Y

DO - 10.1016/0896-6273(93)90065-Y

M3 - Article

C2 - 7686381

AN - SCOPUS:0027210625

VL - 10

SP - 1175

EP - 1184

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 6

ER -