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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Bibliographic Details
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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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)01339-3