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First published online June 23, 2005
doi: 10.1242/10.1242/jcs.02485
Commentary |
1 Inserm, U682 Strasbourg, F67200, Development and Physiopathology of the Intestine and Pancreas, University Louis Pasteur, Strasbourg, France
2 Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Département de Pathologie Moléculaire, UPR 6520 CNRS/U596 INSERM, Université Louis Pasteur, BP10142, 67404 Illkirch, C.U. de Strasbourg, France
* Author for correspondence (e-mail: cat{at}igbmc.u-strasbg.fr)
The steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain is a protein module of 
210 residues that binds lipids, including sterols. Fifteen mammalian proteins, STARD1-STARD15, possess a START domain and these can be grouped into six subfamilies. Cholesterol, 25-hydroxycholesterol, phosphatidylcholine, phosphatidylethanolamine and ceramides are ligands for STARD1/STARD3/STARD5, STARD5, STARD2/STARD10, STARD10 and STARD11, respectively. The lipids or sterols bound by the remaining 9 START proteins are unknown. Recent studies show that the C-terminal end of the domain plays a fundamental role, forming a lid over a deep lipid-binding pocket that shields the ligand from the external environment. The START domain can be regarded as a lipid-exchange and/or a lipid-sensing domain. Mammalian START proteins have diverse expression patterns and can be found free in the cytoplasm, attached to membranes or in the nucleus. They appear to function in a variety of distinct physiological processes, such as lipid transfer between intracellular compartments, lipid metabolism and modulation of signaling events. Mutation or misexpression of START proteins is linked to pathological processes, including genetic disorders, autoimmune disease and cancer.
Key words: START, Cholesterol, Phosphatidylcholine, Lipid
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