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Arginine-427 in the Na +/glucose cotransporter (SGLT1) is involved in trafficking to the plasma membrane

To investigate the role of charged intramembrane residues in the function of the rabbit Na +/glucose cotransporter (rbSGLT1) we substituted arginine-427 (R427) by alanine in the putative domain M9 SGLT1. This residue is conserved in all the members of the SGLT1 family. The mutant protein (R427A) was...

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Published in:	FEBS letters 1995-12, Vol.377 (2), p.181-184
Main Authors:	Lostao, M.Pilar, Hirayama, Bruce A., Panayotova-Heiermann, Mariana, Sampogna, Sharon L., Bok, Dean, Wright, Ernest M.
Format:	Article
Language:	English
Subjects:	Animals Arginine - metabolism Base Sequence Binding Sites Biological Transport Cell Membrane - metabolism Electrophysiology Freeze-fracture Glucose - metabolism Heterologous expression Immunocytochemistry Membrane Glycoproteins Membrane Proteins - chemistry Membrane Proteins - metabolism Methylglucosides - metabolism Molecular Sequence Data Monosaccharide Transport Proteins - chemistry Monosaccharide Transport Proteins - metabolism Na +/glucose cotransporter trafficking Oocytes Plasma membrane Rabbits Sodium - metabolism Sodium-Glucose Transporter 1 Xenopus
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cited_by	cdi_FETCH-LOGICAL-c4663-9930e6c21b588104ed78e66319c1100bf65705030fd0bfc3b5cc49fba48de4343
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creator	Lostao, M.Pilar Hirayama, Bruce A. Panayotova-Heiermann, Mariana Sampogna, Sharon L. Bok, Dean Wright, Ernest M.
description	To investigate the role of charged intramembrane residues in the function of the rabbit Na +/glucose cotransporter (rbSGLT1) we substituted arginine-427 (R427) by alanine in the putative domain M9 SGLT1. This residue is conserved in all the members of the SGLT1 family. The mutant protein (R427A) was expressed in Xenopus oocytes and, although Western blot analysis revealed that it was produced in amounts comparable to wildtype, no function was measured. Freeze-fracture analysis showed that R427A SGLT1 was not in the plasma membrane while immunocytochemical experiments localized the transporter to just beneath it. These results indicate that arginine-427 plays a critical role in SGLT1 trafficking to the plasma membrane.
doi_str_mv	10.1016/0014-5793(95)01339-3
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subjects	Animals Arginine - metabolism Base Sequence Binding Sites Biological Transport Cell Membrane - metabolism Electrophysiology Freeze-fracture Glucose - metabolism Heterologous expression Immunocytochemistry Membrane Glycoproteins Membrane Proteins - chemistry Membrane Proteins - metabolism Methylglucosides - metabolism Molecular Sequence Data Monosaccharide Transport Proteins - chemistry Monosaccharide Transport Proteins - metabolism Na +/glucose cotransporter trafficking Oocytes Plasma membrane Rabbits Sodium - metabolism Sodium-Glucose Transporter 1 Xenopus
title	Arginine-427 in the Na +/glucose cotransporter (SGLT1) is involved in trafficking to the plasma membrane
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