The apical sorting signal for human GLUT9b resides in the N-terminus

• Published in: Molecular and cellular biochemistry Vol. 376; no. 1-2; pp. 163 - 173
• Main Authors: Bibee, Kristin P., Augustin, Robert, Gazit, Vered, Moley, Kelle H.
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01.04.2013; Springer; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Biochemistry; Biomedical and Life Sciences; Cardiology; Cell Line; Cell Membrane - metabolism; Dextrose; Dogs; Glucose; Glucose metabolism; Glucose Transport Proteins, Facilitative - genetics; Glucose Transport Proteins, Facilitative - metabolism; Humans; Leucine - metabolism; Life Sciences; Medical Biochemistry; Membranes; Molecular biology; Molecular Sequence Data; Mutation; Oncology; Protein Sorting Signals; Protein Transport; Proteins; Glucose transporter; Targeting; Plasma membrane

The two splice variants of human glucose transporter 9 (hGLUT9) are targeted to different polarized membranes. hGLUT9a traffics to the basolateral membrane, whereas hGLUT9b traffics to the apical region. This study examines the sorting mechanism of these variants, which differ only in their N-termin...