TAILIEUCHUNG - Báo cáo khoa học: Lysosomal localization of GLUT8 in the testis – the EXXXLL motif of GLUT8 is sufficient for its intracellular sorting via AP1- and AP2-mediated interaction

The class III sugar transport facilitator GLUT8 co-localizes with the lyso-somal protein LAMP1 in heterologous expression systems. GLUT8 carries a [D⁄E]XXXL[L⁄I]-type dileucine sorting signal that has been postulated to retain the protein in an endosomal⁄lysosomal compartment via interactions with clathrin adaptor protein (AP) complexes. | Lysosomal localization of GLUT8 in the testis - the EXXXLL motif of GLUT8 is sufficient for its intracellular sorting via AP1- and AP2-mediated interaction Muhammed Kasim Diril1 Stefan Schmidt2 Michael KrauB1 Verena Gawlik2 Hans-Georg Joost2 Annette Schurmann2 Volker Haucke1 and Robert Augustin2 1 Institute of Chemistry and Biochemistry Department of Membrane Biochemistry Freie Universitat Charite Universitatsmedizin Berlin Takustrasse 6 Berlin Germany 2 Department of Pharmacology German Institute of Human Nutrition Potsdam Rehbruecke Arthur-Scheunert-Allee 114-116 Nuthetal Germany Keywords adaptor proteins endocytosis glucose transporter GLUT8 lysosomes targeting Correspondence R. Augustin Department of Cardiometabolic Diseases Research Boehringer-Ingelheim Pharma GmbH Co KG Birkendorferstrasse 65 88397 Biberach an der Riss Germany Fax 49 7351 542187 Tel 49 7351 545252 E-mail Re-use of this article is permitted in accordance with the Terms and Conditions set out at http . authorresources Received 17 November 2008 revised 25 April2009 accepted 11 May 2009 doi The class III sugar transport facilitator GLUT8 co-localizes with the lysosomal protein LAMP1 in heterologous expression systems. GLUT8 carries a D E XXXL L I -type dileucine sorting signal that has been postulated to retain the protein in an endosomal lysosomal compartment via interactions with clathrin adaptor protein AP complexes. However contradictory findings have been described regarding the subcellular localization of the endogenous GLUT8 and the adaptor proteins that interact with its dileucine motif. Here we demonstrate that endogenous GLUT8 is localized in a late endoso-mal lysosomal compartment of spermatocytes and spermatids and that the adaptor complexes AP1 and AP2 but not AP3 or AP4 interact with its N-terminal intracellular domain NICD . In addition fusion of the GLUT8 NICD to .

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