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Journal of Lipid Research, Vol. 50, S299-S304, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Membranes and Lipid Domains

Lipid binding domains: more than simple lipid effectors

Robert V. Stahelin¹

Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, Raclin-Carmichael Hall, 1234 Notre Dame Avenue, South Bend, IN 46617; and Department of Chemistry and Biochemistry and The Walther Center for Cancer Research, University of Notre Dame, Notre Dame, IN 46556

This research was supported by grants from the American Heart Association (0735350N), the American Cancer Society (IRG-84-002-22), and the Indiana University School of Medicine.

Published, JLR Papers in Press, November 13, 2008.

¹ To whom correspondence should be addressed. e-mail: rstaheli{at}iupui.edu

ABSTRACT

The spatial and temporal regulation of lipid molecules in cell membranes is a hallmark of cellular signaling and membrane trafficking events. Lipid-mediated targeting provides for strict control and versatility, because cell membranes harbor a large number of lipid molecules with variation in head group and acyl chain structures. Signaling and trafficking proteins contain a large number of modular domains that exhibit specific lipid binding properties and play a critical role in their localization and function. Nearly 20 years of research including structural, computational, biochemical and biophysical studies have demonstrated how these lipid-binding domains recognize their target lipid and achieve subcellular localization. The integration of this individual lipid-binding domain data in the context of the full-length proteins, macromolecular signaling complexes, and the lipidome is only beginning to be unraveled and represents a target of therapeutic development. This review brings together recent findings and classical concepts to concisely summarize the lipid-binding domain field while illustrating where the field is headed and how the gaps may be filled in with new technologies.

Supplementary key words C1 domain • C2 domain • peripheral protein

Abbreviations: cPLA₂, cytosolic phospholipase A₂; DAG, diacylglycerol; FCS, fluorescence correlation spectroscopy; GFP, green fluorescent protein; PH, pleckstrin homology; PI, phosphoinositide; PIP₃ or PtdIns(3,4,5)P₃, phosphatidylinositol 3,4,5-trisphosphate; PIP₂ or PtdIns(4,5)P₂, phosphatidylinositol 4,5-bisphosphate; PKC, protein kinase C; PM, plasma membrane; PS, phosphatidylserine

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