J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

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
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
R600028-JLR200v1
48/3/489    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Smolenaars, M. M.W.
Right arrow Articles by Van der Horst, D. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smolenaars, M. M.W.
Right arrow Articles by Van der Horst, D. J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.