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A more recent version of this article appeared on March 1, 2007

Papers In Press, published online ahead of print December 5, 2006
J. Lipid Res., doi:10.1194/jlr.R600028-JLR200
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Submitted on October 18, 2006
Revised on November 27, 2006
Accepted on December 4, 2006

Molecular diversity and evolution of the large lipid transfer protein superfamily

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

Biochemical Physiology, Utrecht University, Utrecht, Utrecht NL 3584 CH

Corresponding Author: k.w.rodenburg{at}bio.uu.nl

Circulatory lipid transport in animals is mediated for a substantial part 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, i.e. the apoB-like LLTPs, the vitellogenin (Vtg)-like LLTPs, and the microsomal triglyceride transfer protein (MTP)-like LLTPs or MTPs. The latter are ubiquitous, while 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 additional 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 manipulation of lipid transport.


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