TAILIEUCHUNG - Báo cáo khoa học: Identification of a glycosphingolipid transfer protein GLTP1 in Arabidopsis thaliana

Arabidopsis thaliana At2g33470 encodes a glycolipid transfer protein (GLTP) that enhances the intervesicular trafficking of glycosphingolipids in vitro. GLTPs have previously been identified in animals and fungi but not in plants. Thus, At2g33470 is the first identified plant GLTP and we have designated it AtGTLP1. | ỊFEBS Journal Identification of a glycosphingolipid transfer protein GLTP1 in Arabidopsis thaliana Gun West1 z Lenita Viitanen1 z Christina Alm2 Peter Mattjus1 Tiina A. Salminen1 and Johan Edqvist3 1 Department of Biochemistry and Pharmacy Abo Akademi University Turku Finland 2 Department of Plant Biology and Forest Genetics Swedish University of AgriculturalSciences Uppsala Sweden 3 IFM-Biology Linkoping University Sweden Keywords ceramide GLTP glycolipids lipid transfer sphingolipids Correspondence J. Edqvist IFM-Biology Linkoping University SE-581 83 Linkoping Sweden Fax 46 13 281399 Tel 46 13 281288 E-mail Johed@ These authors contributed equally to this study Received 24 January 2008 revised 12 March 2008 accepted 30 April 2008 doi Arabidopsis thaliana At2g33470 encodes a glycolipid transfer protein GLTP that enhances the intervesicular trafficking of glycosphingolipids in vitro. GLTPs have previously been identified in animals and fungi but not in plants. Thus At2g33470 is the first identified plant GLTP and we have designated it AtGTLP1. AtGLTP1 transferred BODIPY-glucosyl-ceramide at a rate of pmol-s-1 but BODIPY-galactosylceramide and BODIPY-lactosylceramide were transferred slowly with rates below pmol-s-1. AtGLTP1 did not transfer BODIPY-sphingomyelin monogalactosyldiacylglycerol or digalactosyldiacylglycerol. The human GLTP transfers BODIPY-glucosylceramide BODIPY-galactosylceramide and BO-DIPY-lactosylceramide with rates greater than pmol-s-1. Structural models showed that the residues that are most critical for glycosphingolipid binding in human GLTP are conserved in AtGLTP1 but some of the sugar-binding residues are unique and this provides an explanation for the distinctly different transfer preferences of AtGLTP1 and human GLTP. The AtGLTP1 variant Arg59Lys Asn95Leu showed low BODIPY-gluco-sylceramide transfer activity indicating that Arg59 and or Asn95 are important for the specific binding of

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