Abstract:
:Members of the family of intracellular lipid binding proteins (iLBPs) have been implicated in cytoplasmic transport of lipophilic ligands, such as long-chain fatty acids and retinoids. iLBPs are low molecular mass proteins (14-16 kDa) sharing a common structural fold. The iLBP family likely arose through duplication and diversification of an ancestral iLBP gene. Phylogenetic analysis undertaken in the present study indicates that the ancestral iLBP gene arose after divergence of animals from fungi and plants. The first gene duplication was dated around 930 millions of years ago, and subsequent duplications in the succeeding 550 millions of years gave rise to the 16 iLBP types currently recognized in vertebrates. Four clusters of proteins, each binding a characteristic range of ligands, are evident from the phylogenetic tree. Evolution of different binding properties probably allowed cytoplasmic trafficking of distinct ligands. It is speculated that recruitment of an iLBP during evolution of animals enabled the mitochondrial oxidation of long-chain fatty acids.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Schaap FG,van der Vusse GJ,Glatz JFkeywords:
subject
Has Abstractpub_date
2002-10-01 00:00:00pages
69-77issue
1-2eissn
0300-8177issn
1573-4919journal_volume
239pub_type
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