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Molecular characteristics of phosphoinositide binding

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Abstract

Phosphoinositides in general and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2 or PIP2) in particular have been recently found to function as important regulators of ion channels. Yet, while specific residues have been identified that affect channel–PIP2 interactions, the precise binding site of PIP2 has not been determined in any case. In addition to binding ion channels, however, phosphoinositides interact with a plethora of other proteins, and in a number of cases, the crystallographic structures of the complexes have been determined. Based on a database of 25 complexed crystallographic structures, we have addressed the molecular characteristics of phosphoinositide binding to proteins. Implications to phosphoinositide binding to ion channels are also discussed.

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  1. Department of Structural and Chemical Biology, Mount Sinai School of Medicine, New York, NY, 10029, USA

    Avia Rosenhouse-Dantsker & Diomedes E. Logothetis

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  1. Avia Rosenhouse-Dantsker
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  2. Diomedes E. Logothetis
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Correspondence to Avia Rosenhouse-Dantsker.

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Rosenhouse-Dantsker, A., Logothetis, D.E. Molecular characteristics of phosphoinositide binding. Pflugers Arch - Eur J Physiol 455, 45–53 (2007). https://doi.org/10.1007/s00424-007-0291-6

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