Glucose binding enhances the papain susceptibility of the intracellular loop of the GLUT1 glucose transporter

Tomoichiro Asano, Hideki Katagiri, Katsunori Tsukuda, Jiann Liang Lin, Hisamitsu Ishihara, Kouichi Inukai, Yoshio Yazaki, Yoshitomo Oka

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Digestion of human GLUT1 protein in erythrocytes with 5 μg/ml papain for 5 min yielded several fragments. By using several site-specific antibodies, two of these fragments containing the intracellular loop domain between M6 and M7 were demonstrated to be further digested by a prolonged incubation with papain. The addition of 0.2 M d-glucose enhanced this digestion between M6 and M7 by approximately 3.5-fold, while the addition of 0.2 M d-sorbitol exhibited no effects. These results strongly suggest that d-glucose binding induces the conformational change of the intracellular loop domain between M6 and M7 of GLUT1 protein. Since the homology of the amino acid sequence was low in this intracellular domain among the five facilitative glucose transporter isoforms, this intracellular loop might contribute to the difference in their Km and Vmax values for glucose uptake.

Original languageEnglish
Pages (from-to)129-132
Number of pages4
JournalFEBS Letters
Volume298
Issue number2-3
DOIs
Publication statusPublished - 1992 Feb 24
Externally publishedYes

Keywords

  • GLUT1
  • Glucose
  • Glucose transporter
  • Papain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Glucose binding enhances the papain susceptibility of the intracellular loop of the GLUT1 glucose transporter'. Together they form a unique fingerprint.

Cite this