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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.R800084-JLR200 on November 17, 2008

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Journal of Lipid Research, Vol. 50, S126-S131, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Metabolism

Structural and functional analysis of fatty acid-binding proteins

Judith Storch1,* and Lindsay McDermott{dagger}

* Department of Nutritional Sciences, Rutgers Center for Lipid Research, Rutgers University, New Brunswick, NJ 08901
{dagger} Pharmaceutical Science Division, School of Biomedical and Health Sciences, King's College, London SE1 9NH United Kingdom

Published, JLR Papers in Press, November 17, 2008.

1 To whom correspondence should be addressed. e-mail: storch{at}aesop.rutgers.edu


ABSTRACT

The mammalian FA-binding proteins (FABPs) bind long-chain FA with high affinity. The large number of FABP types is suggestive of distinct functions in specific tissues. Multiple experimental approaches have shown that individual FABPs possess both unique and overlapping functions, some of which are based on specific elements in the protein structure. Although FA binding affinities for all FABPs tend to correlate directly with FA hydrophobicity, structure-function studies indicate that subtle three-dimensional changes that occur upon ligand binding may promote specific protein-protein or protein-membrane interactions that ultimately determine the function of each FABP. The conformational changes are focused in the FABP helical/portal domain, a region that was identified by in vitro studies to be vital for the FA transport properties of the FABPs. Thus, the FABPs modulate intracellular lipid homeostasis by regulating FA transport in the nuclear and extra-nuclear compartments of the cell; in so doing, they also impact systemic energy homeostasis.

Supplementary key words lipid-binding proteins • lipid transport • transcription factors • protein-membrane interactions

Abbreviations: AFABP, adipocyte FA-binding protein; CRABPII, cellular retinoic acid binding protein II; DHA, docosahexaenoic acid; DKO, double knockout; FABP, FA-binding protein; HFABP, heart/muscle FA-binding protein; IFABP, intestinal FA-binding protein; HSL, hormone-sensitive lipase; KFABP, keratinocyte FA-binding protein; LFABP, liver FA-binding protein; NLS, nuclear localization signal; PPAR, peroxisome proliferator activated receptor; RA, retinoic acid; RAR, retinoic acid receptor


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Related Webpages:

JLR 50th Anniversary Collections
Anniversary Collection:: Metabolism



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