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Papers In Press, published online ahead of print March 1, 2007
J. Lipid Res., doi:10.1194/jlr.R600028-JLR200

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Journal of Lipid Research, Vol. 48, 489-502, March 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Review

Molecular diversity and evolution of the large lipid transfer protein superfamily

Marcel M. W. Smolenaars^*, Ole Madsen, Kees W. Rodenburg^1,* and Dick J. Van der Horst^*

^* Biochemical Physiology, Department of Biology and Institute of Biomembranes, Faculty of Science, Utrecht University, Utrecht, The Netherlands
Department of Biochemistry, Faculty of Science, Radboud University, Nijmegen, The Netherlands

The online version of this article (available at http://www.jlr.org) contains supplemental data.

Published, JLR Papers in Press, December 5, 2006.

¹ To whom correspondence should be addressed. e-mail: k.w.rodenburg{at}bio.uu.nl

Circulatory lipid transport in animals is mediated to a substantial extent by members of the large lipid transfer (LLT) protein (LLTP) superfamily. These proteins, including apolipoprotein B (apoB), bind lipids and constitute the structural basis for the assembly of lipoproteins. The current analyses of sequence data indicate that LLTPs are unique to animals and that these lipid binding proteins evolved in the earliest multicellular animals. In addition, two novel LLTPs were recognized in insects. Structural and phylogenetic analyses reveal three major families of LLTPs: the apoB-like LLTPs, the vitellogenin-like LLTPs, and the microsomal triglyceride transfer protein (MTP)-like LLTPs, or MTPs. The latter are ubiquitous, whereas the two other families are distributed differentially between animal groups. Besides similarities, remarkable variations are also found among LLTPs in their major lipid-binding sites (i.e., the LLT module as well as the predicted clusters of amphipathic secondary structure): variations such as protein modification and number, size, or occurrence of the clusters. Strikingly, comparative research has also highlighted a multitude of functions for LLTPs in addition to circulatory lipid transport. The integration of LLTP structure, function, and evolution reveals multiple adaptations, which have come about in part upon neofunctionalization of duplicated genes. Moreover, the change, exchange, and expansion of functions illustrate the opportune application of lipid-binding proteins in nature. Accordingly, comparative research exposes the structural and functional adaptations in animal lipid carriers and brings up novel possibilities for the manipulation of lipid transport.

Supplementary key words phylogeny • subfunctionalization • sequence alignment • clotting protein • melanin-engaging protein • microsomal triglyceride transfer protein • von Willebrand factor • lipophorin • apolipoprotein B • vitellogenin • lipid droplet

Abbreviations: aa, amino acids; apoB, apolipoprotein B; apoLp, apolipophorin; ARP, apolipophorin-II/I-related protein; CP, clotting protein; LLT, large lipid transfer; LLTP, large lipid transfer protein; MEP, melanin-engaging protein; MTP, microsomal triglyceride transfer protein; PDI, protein disulfide isomerase; Vtg, vitellogenin; vWF, von Willebrand factor

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