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Title: Competitive cation binding to phosphatidylinositol-4,5-bisphosphate domains revealed by X-ray fluorescence

Abstract

Calcium ions bind strongly to PIP 2at physiological concentrations, leading to condensation and decreased effective charge for PIP 2. Calcium displaces the more numerous magnesium and potassium ions, but some potassium ions remain.

Authors:
 [1];  [2];  [3];  [4];  [2];  [5]
  1. Department of Chemistry and Biochemistry; Kent State University; Kent; USA
  2. Ames Laboratory and Department of Physics and Astronomy; Iowa State University; Ames; USA
  3. Department of Physics; Kent State University; Kent; USA
  4. X-ray Science Division; Advanced Photon Source; Argonne National Laboratory; Lemont; USA
  5. Department of Biological Sciences; Kent State University; Kent; USA
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1415472
DOE Contract Number:  
AC02-06CH11357
Resource Type:
Journal Article
Journal Name:
RSC Advances
Additional Journal Information:
Journal Volume: 5; Journal Issue: 129; Journal ID: ISSN 2046-2069
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Graber, Z. T., Wang, W., Singh, G., Kuzmenko, I., Vaknin, D., and Kooijman, E. E. Competitive cation binding to phosphatidylinositol-4,5-bisphosphate domains revealed by X-ray fluorescence. United States: N. p., 2015. Web. doi:10.1039/c5ra19023a.
Graber, Z. T., Wang, W., Singh, G., Kuzmenko, I., Vaknin, D., & Kooijman, E. E. Competitive cation binding to phosphatidylinositol-4,5-bisphosphate domains revealed by X-ray fluorescence. United States. doi:10.1039/c5ra19023a.
Graber, Z. T., Wang, W., Singh, G., Kuzmenko, I., Vaknin, D., and Kooijman, E. E. Thu . "Competitive cation binding to phosphatidylinositol-4,5-bisphosphate domains revealed by X-ray fluorescence". United States. doi:10.1039/c5ra19023a.
@article{osti_1415472,
title = {Competitive cation binding to phosphatidylinositol-4,5-bisphosphate domains revealed by X-ray fluorescence},
author = {Graber, Z. T. and Wang, W. and Singh, G. and Kuzmenko, I. and Vaknin, D. and Kooijman, E. E.},
abstractNote = {Calcium ions bind strongly to PIP2at physiological concentrations, leading to condensation and decreased effective charge for PIP2. Calcium displaces the more numerous magnesium and potassium ions, but some potassium ions remain.},
doi = {10.1039/c5ra19023a},
journal = {RSC Advances},
issn = {2046-2069},
number = 129,
volume = 5,
place = {United States},
year = {2015},
month = {1}
}

Works referenced in this record:

Ionization Properties of Phosphatidylinositol Polyphosphates in Mixed Model Membranes
journal, October 2009

  • Kooijman, Edgar E.; King, Katrice E.; Gangoda, Mahinda
  • Biochemistry, Vol. 48, Issue 40
  • DOI: 10.1021/bi9008616

Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment
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  • Nature Structural & Molecular Biology, Vol. 20, Issue 6
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Some simple ideas on X-ray reflection and grazing-incidence diffraction from thin surfactant films
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Phosphoinositides regulate ion channels
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  • Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, Vol. 1851, Issue 6
  • DOI: 10.1016/j.bbalip.2014.09.010

Phosphoinositides in cell regulation and membrane dynamics
journal, October 2006