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Plasma membrane phosphoinositide organization by protein electrostatics

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  • Stuart McLaughlin

    (Health Sciences Center, Stony Brook University)

  • Diana Murray

    (Weill Medical College of Cornell University)

Abstract

Phosphatidylinositol 4,5-bisphosphate (PIP2), which comprises only about 1% of the phospholipids in the cytoplasmic leaflet of the plasma membrane, is the source of three second messengers, activates many ion channels and enzymes, is involved in both endocytosis and exocytosis, anchors proteins to the membrane through several structured domains and has other roles. How can a single lipid in a fluid bilayer regulate so many distinct physiological processes? Spatial organization might be the key to this. Recent studies suggest that membrane proteins concentrate PIP2 and, in response to local increases in intracellular calcium concentration, release it to interact with other biologically important molecules.

Suggested Citation

  • Stuart McLaughlin & Diana Murray, 2005. "Plasma membrane phosphoinositide organization by protein electrostatics," Nature, Nature, vol. 438(7068), pages 605-611, December.
  • Handle: RePEc:nat:nature:v:438:y:2005:i:7068:d:10.1038_nature04398
    DOI: 10.1038/nature04398
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    Cited by:

    1. Yuri N Antonenko & Andreas Horner & Peter Pohl, 2012. "Electrostatically Induced Recruitment of Membrane Peptides into Clusters Requires Ligand Binding at Both Interfaces," PLOS ONE, Public Library of Science, vol. 7(12), pages 1-8, December.

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