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Vol. 10, Issue 4, 819-832, April 1999
The Department of Biochemistry and Molecular Biology, Louisiana
State University School of Medicine, Shreveport, Louisiana 71130-3932
Subcellular targeting and the activity of facilitative glucose
transporters are likely to be regulated by interactions with cellular
proteins. This report describes the identification and characterization
of a protein, GLUT1 C-terminal binding protein (GLUT1CBP), that
binds via a PDZ domain to the C terminus of GLUT1. The interaction
requires the C-terminal four amino acids of GLUT1 and is isoform
specific because GLUT1CBP does not interact with the C terminus of
GLUT3 or GLUT4. Most rat tissues examined contain both GLUT1CBP and
GLUT1 mRNA, whereas only small intestine lacked detectable GLUT1CBP
protein. GLUT1CBP is also expressed in primary cultures of neurons and
astrocytes, as well as in Chinese hamster ovary, 3T3-L1,
Madin-Darby canine kidney, Caco-2, and pheochromocytoma-12 cell lines.
GLUT1CBP is able to bind to native GLUT1 extracted from cell membranes,
self-associate, or interact with the cytoskeletal proteins myosin VI,
-actinin-1, and the kinesin superfamily protein KIF-1B. The
presence of a PDZ domain places GLUT1CBP among a growing family of
structural and regulatory proteins, many of which are localized to
areas of membrane specialization. This and its ability to interact with
GLUT1 and cytoskeletal proteins implicate GLUT1CBP in cellular
mechanisms for targeting GLUT1 to specific subcellular sites either by
tethering the transporter to cytoskeletal motor proteins or by
anchoring the transporter to the actin cytoskeleton.
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