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2017 ; 1864
(9
): 1439-1449
Nephropedia Template TP
Biochim Biophys Acta Mol Cell Res
2017[Sep]; 1864
(9
): 1439-1449
PMID28554774
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Tubular lipid binding proteins (TULIPs) have become a focus of interest in the
cell biology of lipid signalling, lipid traffic and membrane contact sites. Each
tubular domain has an internal pocket with a hydrophobic lining that can bind a
hydrophobic molecule such as a lipid. This allows TULIP proteins to carry lipids
through the aqueous phase. TULIP domains were first found in a large family of
extracellular proteins related to the bacterial permeability-inducing protein
(BPI) and cholesterol ester transfer protein (CETP). Since then, the same fold
and lipid transfer capacity have been found in SMP domains (so-called for their
occurrence in synaptotagmin, mitochondrial and lipid binding proteins), which
localise to intracellular membrane contact sites. Here the methods for
identifying known TULIPs are described, and used to find previously unreported
TULIPs, one in the silk polymer and another in prokaryotes illustrated by the E.
coli protein YceB. The bacterial TULIP alters views on the likely evolution of
the domain, suggesting its presence in the last universal common ancestor. The
major function of TULIPs is to handle lipids, but we still do not know how they
work in detail, or how many more remain to be discovered. This article is part of
a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann
and Benoit Kornmann.
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