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Expression of caveolin‐1 in lymphocytes induces caveolae formation and recruitment of phosphofructokinase to the plasma membrane
Author(s) -
Vallejo Johana,
Hardin Christopher D.
Publication year - 2005
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.04-2380fje
Subject(s) - caveolae , phosphofructokinase , colocalization , microbiology and biotechnology , glycolysis , transfection , caveolin 1 , biology , biochemistry , membrane protein , chemistry , membrane , enzyme , gene
Compartmentation of carbohydrate metabolism has been shown in a wide range of tissues including reports of one compartment of glycolysis associated with the plasma membrane of cells. However, only in the erythrocyte has the physical basis for plasma membrane‐associated glycolytic pathway been established. We have previously found that phosphofructokinase (PFK) appeared to colocalize with the fairly ubiquitous plasma membrane protein caveolin‐1 (CAV‐1), consistent with a role for CAV‐1 as an anchor for glycolysis to the plasma membrane. To test the hypothesis that CAV‐1 functions as a scaffolding protein for PFK, we transfected human lymphocytes (a cell without CAV‐1 expression) with human CAV‐1 cDNA. We demonstrate that expression of CAV‐1 in lymphocytes results in the formation of caveolae at the plasma membrane and affects the subcellular localization of PFK by recruiting PFK to the plasma membrane. Targeting of PFK by CAV‐1 also was validated by the significant colocalization between the proteins after transfection, which resulted in a correlation of 0.97 ± 0.004 between the two fluorophores. This finding is significant in as much as it illustrates the CAV‐1 feasibility of generating binding sites for glycolytic enzymes on the plasma membrane. We therefore conclude that CAV‐1 functions as a scaffolding protein for PFK and that this may contribute to the elucidation of the basis for carbohydrate compartmentation to the plasma membrane in a wide variety of cell types.