TY - JOUR
T1 - Evidence for three populations of the glucose transporter in the human erythrocyte membrane
AU - Kodippili, Gayani C.
AU - Putt, Karson S.
AU - Low, Philip S.
N1 - Publisher Copyright:
© 2019 Elsevier Inc.
PY - 2019/7
Y1 - 2019/7
N2 - Glucose transporter 1 (GLUT1) is one of 13 members of the human equilibrative glucose transport protein family and the only glucose transporter thought to be expressed in human erythrocyte membranes. Although GLUT1 has been shown to be anchored to adducin at the junctional spectrin-actin complex of the membrane through interactions with multiple proteins, whether other populations of GLUT1 also exist in the human erythrocyte membrane has not been examined. Because GLUT1 plays such a critical role in erythrocyte biology and since it comprises 10% of the total membrane protein, we undertook to evaluate the subpopulations of erythrocyte GLUT1 using single particle tracking. By monitoring the diffusion of individual AlexaFluor 488-labeled GLUT1 molecules on the surfaces of intact erythrocytes, we are able to identify three distinct subpopulations of GLUT1. While the mobility of the major subpopulation is similar to that of the anion transporter, band 3, both a more mobile and more anchored subpopulation also exist. From these studies, we conclude that ~65% of GLUT1 resides in similar or perhaps the same protein complex as band 3, while the remaining 1/3rd are either freely diffusing or interacting with other cytoskeletally anchored membrane protein complexes.
AB - Glucose transporter 1 (GLUT1) is one of 13 members of the human equilibrative glucose transport protein family and the only glucose transporter thought to be expressed in human erythrocyte membranes. Although GLUT1 has been shown to be anchored to adducin at the junctional spectrin-actin complex of the membrane through interactions with multiple proteins, whether other populations of GLUT1 also exist in the human erythrocyte membrane has not been examined. Because GLUT1 plays such a critical role in erythrocyte biology and since it comprises 10% of the total membrane protein, we undertook to evaluate the subpopulations of erythrocyte GLUT1 using single particle tracking. By monitoring the diffusion of individual AlexaFluor 488-labeled GLUT1 molecules on the surfaces of intact erythrocytes, we are able to identify three distinct subpopulations of GLUT1. While the mobility of the major subpopulation is similar to that of the anion transporter, band 3, both a more mobile and more anchored subpopulation also exist. From these studies, we conclude that ~65% of GLUT1 resides in similar or perhaps the same protein complex as band 3, while the remaining 1/3rd are either freely diffusing or interacting with other cytoskeletally anchored membrane protein complexes.
KW - Band 3
KW - Erythrocyte membrane structure
KW - GLUT1
KW - Glucose transporter 1
KW - Single particle tracking
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U2 - 10.1016/j.bcmd.2019.03.005
DO - 10.1016/j.bcmd.2019.03.005
M3 - Article
C2 - 30974390
AN - SCOPUS:85063876073
SN - 1079-9796
VL - 77
SP - 61
EP - 66
JO - Blood Cells, Molecules, and Diseases
JF - Blood Cells, Molecules, and Diseases
ER -