PMID- 10198040
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20200204
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 4
DP  - 1999 Apr
TI  - Protein interactions with the glucose transporter binding protein GLUT1CBP that
      provide a link between GLUT1 and the cytoskeleton.
PG  - 819-32
AB  - 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, 
      alpha-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.
FAU - Bunn, R C
AU  - Bunn RC
AD  - The Department of Biochemistry and Molecular Biology, Louisiana State University 
      School of Medicine, Shreveport, Louisiana 71130-3932, USA.
FAU - Jensen, M A
AU  - Jensen MA
FAU - Reed, B C
AU  - Reed BC
LA  - eng
SI  - GENBANK/AF032120
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (GIPC1 protein, human)
RN  - 0 (Gipc1 protein, mouse)
RN  - 0 (Gipc1 protein, rat)
RN  - 0 (Glucose Transporter Type 1)
RN  - 0 (Monosaccharide Transport Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (SLC2A1 protein, human)
RN  - 0 (Slc2a1 protein, mouse)
RN  - 0 (Slc2a1 protein, rat)
SB  - IM
MH  - 3T3 Cells
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Astrocytes/metabolism
MH  - Base Sequence
MH  - CHO Cells
MH  - Carrier Proteins/chemistry/genetics/*metabolism
MH  - Cell Line
MH  - Cricetinae
MH  - Cytoskeleton/*metabolism
MH  - Dogs
MH  - Glucose Transporter Type 1
MH  - Humans
MH  - Male
MH  - Mice
MH  - Molecular Sequence Data
MH  - Monosaccharide Transport Proteins/genetics/*metabolism
MH  - Neurons/metabolism
MH  - *Neuropeptides
MH  - Organ Specificity
MH  - Pheochromocytoma
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Recombinant Proteins/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transfection
MH  - Tumor Cells, Cultured
PMC - PMC25204
EDAT- 1999/04/10 00:00
MHDA- 1999/04/10 00:01
CRDT- 1999/04/10 00:00
PHST- 1999/04/10 00:00 [pubmed]
PHST- 1999/04/10 00:01 [medline]
PHST- 1999/04/10 00:00 [entrez]
AID - 10.1091/mbc.10.4.819 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Apr;10(4):819-32. doi: 10.1091/mbc.10.4.819.