title: Sphingolipid transfer proteins defined by the GLTP-fold.
abstract: Glycolipid transfer proteins (GLTPs) originally were identified as small (~24 kDa), soluble, amphitropic proteins that specifically accelerate the intermembrane transfer of glycolipids. GLTPs and related homologs now are known to adopt a unique, helically dominated, two-layer 'sandwich' architecture defined as the GLTP-fold that provides the structural underpinning for the eukaryotic GLTP superfamily. Recent advances now provide exquisite insights into structural features responsible for lipid headgroup selectivity as well as the adaptability of the hydrophobic compartment for accommodating hydrocarbon chains of differing length and unsaturation. A new understanding of the structural versatility and evolutionary premium placed on the GLTP motif has emerged. Human GLTP-motifs have evolved to function not only as glucosylceramide binding/transferring domains for phosphoinositol 4-phosphate adaptor protein-2 during glycosphingolipid biosynthesis but also as selective binding/transfer proteins for ceramide-1-phosphate. The latter, known as ceramide-1-phosphate transfer protein, recently has been shown to form GLTP-fold while critically regulating Group-IV cytoplasmic phospholipase A2 activity and pro-inflammatory eicosanoid production.
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: Lucy
authors: L
authors: Malinina
authors: Structural Biology Program,Memorial Sloan-Kettering Cancer Center,New York,NY 10065,USA.
authors: Dhirendra K
authors: DK
authors: Simanshu
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: Xiuhong
authors: X
authors: Zhai
authors: Structural Biology Unit,CICbioGUNE, Technology Park of Bizkaia,48160 Derio-Bilbao,Spain.
authors: Valeria R
authors: VR
authors: Samygina
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: RaviKanth
authors: R
authors: Kamlekar
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: Roopa
authors: R
authors: Kenoth
authors: Structural Biology Unit,CICbioGUNE, Technology Park of Bizkaia,48160 Derio-Bilbao,Spain.
authors: Borja
authors: B
authors: Ochoa-Lizarralde
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: Margarita L
authors: ML
authors: Malakhova
authors: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry,Russian Academy of Sciences,Moscow,Russia.
authors: Julian G
authors: JG
authors: Molotkovsky
authors: Structural Biology Program,Memorial Sloan-Kettering Cancer Center,New York,NY 10065,USA.
authors: Dinshaw J
authors: DJ
authors: Patel
authors: The Hormel Institute, University of Minnesota,Austin,MN 55912,USA.
authors: Rhoderick E
authors: RE
authors: Brown
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism*; D006017:Glycolipids / Q000378:metabolism; D017510:Protein Folding; D013107:Sphingolipids / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D006017:Glycolipids; D013107:Sphingolipids