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Science 6 September 1985:
Vol. 229. no. 4717, pp. 941 - 945
DOI: 10.1126/science.3839598
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Articles

Science, Vol 229, Issue 4717, 941-945
Copyright © 1985 by American Association for the Advancement of Science

articles

Sequence and structure of a human glucose transporter

M Mueckler, C Caruso, SA Baldwin, M Panico, I Blench, HR Morris, WJ Allard, GE Lienhard, and HF Lodish

The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.


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Multiple mechanisms of protein insertion into and across membranes.
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Deregulation of Glucose Transporter 1 and Glycolytic Gene Expression by c-Myc.
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A Three-dimensional Model of the Human Facilitative Glucose Transporter Glut1.
F. A. Zuniga, G. Shi, J. F. Haller, A. Rubashkin, D. R. Flynn, P. Iserovich, and J. Fischbarg (2001)
J. Biol. Chem. 276, 44970-44975
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Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes.
C. J. Woodrow, R. J. Burchmore, and S. Krishna (2000)
PNAS 97, 9931-9936
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Science. ISSN 0036-8075 (print), 1095-9203 (online)