tailieunhanh - Báo cáo khoa học: The intrinsic structure of glucose transporter isoforms Glut1 and Glut3 regulates their differential distribution to detergent-resistant membrane domains in nonpolarized mammalian cells

The hexose transporter family, which mediates facilitated uptake in mammalian cells, consists of more than 10 members containing 12 mem-brane-spanning segments with a single N-glycosylation site. We previously demonstrated that glucose transporter 1 is organized into a raft-like deter-gent-resistant membrane domain but that glucose transporter 3 distributes to fluid membrane domains in nonpolarized mammalian cells. | ỊFEBS Journal The intrinsic structure of glucose transporter isoforms Glutl and Glut3 regulates their differential distribution to detergent-resistant membrane domains in nonpolarized mammalian cells Tomoko Sakyo1 2 Hiroaki Naraba1 Hirobumi Teraoka2 and Takayuki Kitagawa1 3 1 PharmaceuticalResearch Center Iwate MedicalUniversity Morioka Japan 2 Department of PathologicalBiochemistry MedicalResearch Institute Tokyo Medicaland DentalUniversity Tokyo Japan 3 Department of Biochemistry and Cell Biology NationalInstitute of Infectious Diseases Tokyo Japan Keywords detergent-resistant membrane glucose transporter 1 glucose transporter 3 mammalian glucose transporter sorting signal Correspondence T. Kitagawa Department of Cell Biology and Molecular Pathology Iwate Medical University Schoolof Pharmacy Iwate 028-3694 Japan Fax 81 19 698 1844 Tel 81 19 651 5111 Ext. 5150 E-mail tkitaga@ Received 23 January 2007 revised 9 March 2007 accepted 30 March 2007 doi The hexose transporter family which mediates facilitated uptake in mammalian cells consists of more than 10 members containing 12 membrane-spanning segments with a single N-glycosylation site. We previously demonstrated that glucose transporter 1 is organized into a raft-like detergent-resistant membrane domain but that glucose transporter 3 distributes to fluid membrane domains in nonpolarized mammalian cells. In this study we further examined the structural basis responsible for the distribution by using a series of chimeric constructs. Glucose transporter 1 and glucose transporter 3 with a FLAG-tagged N-terminus were expressed in detergentresistant membranes and non-detergent-resistant membranes of CHO-K1 cells respectively. Replacement of either the C-terminal or N-terminal cytosolic portion of FLAG-tagged glucose transporter 1 and glucose transporter 3 did not affect the membrane distribution. However a critical sorting signal may exist within the N-terminal half of .

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