The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex.

Recent work identified ABCA1 as the major regulator of plasma HDL-cholesterol responsible for the removal of excess choline-phospholipids and cholesterol from peripheral cells and tissues. ABCA1 function may depend on the association with heteromeric proteins and to identify these candidates a human liver yeast two-hybrid library was screened with the ...
carboxyterminal 144 amino acids of ABCA1. Beta2-syntrophin was found to interact with ABCA1 and the C-terminal five amino acids of ABCA1 proned to represent a perfect tail for binding to syntrophin PDZ domains. Immunoprecipitation further confirmed the association of ABCA1 and beta2-syntrophin and in addition utrophin, known to couple beta2-syntrophin and its PDZ ligands to the F-actin cytoskeleton, was identified as a constituent of this complex. ABCA1 in the plasmamembrane of human macrophages was found to be partially associated with Lubrol rafts and effluxed choline-phospholipids involve these microdomains. Beta2-syntrophin does not colocalize in these rafts indicating that beta2-syntrophin may participate in the retaining of ABCA1 in cytoplasmic vesicles and for the targeting of ABCA1 to plasmamembrane microdomains when ABCA1 is released from beta2-syntrophin.
Mesh Terms:
ATP-Binding Cassette Transporters, Adult, Amino Acid Sequence, Cell Membrane, Cells, Cultured, Cytoplasmic Vesicles, Cytoskeletal Proteins, Dystrophin-Associated Proteins, Fibroblasts, Humans, Macromolecular Substances, Membrane Proteins, Middle Aged, Molecular Sequence Data, Precipitin Tests, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Two-Hybrid System Techniques, Utrophin
Biochem. Biophys. Res. Commun.
Date: May. 03, 2002
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