The actin cytoskeleton mediates the hormonally regulated translocation of type II iodothyronine 5'-deiodinase in astrocytes
Department of Nuclear Medicine; Department of Medicine, Division of Endocrinology & Metabolism; Department of Physiology
Actins; Affinity Labels; Animals; Astrocytes; Biological Transport; Bucladesine; Cell Compartmentation; Cell Membrane; Cytoskeleton; Fluorescent Antibody Technique; Intracellular Membranes; Iodide Peroxidase; Membrane Proteins; Rats; Rats, Inbred Strains; Subcellular Fractions; Thyroxine
Life Sciences | Medicine and Health Sciences
Thyroid hormone, specifically thyroxine, alters cytoskeletal organization in astrocytes by modulating actin polymerization and, in turn, regulates the turnover of the short-lived membrane protein, type II iodothyronine 5'-deiodinase. In the absence of thyroxine, approximately 35% of the total cellular actin is depolymerized, and greater than 90% of the deiodinase is found in the plasma membrane and not associated with the cytoskeleton. Addition of thyroxine promotes actin polymerization and decreases the depolymerized actin to approximately 10% of the total actin pool, induces binding of the deiodinase to F-actin, and promotes rapid internalization of the enzyme. These data provide direct evidence that the actin cytoskeleton participates in the inactivation pathway of the deiodinase by translocating this short-lived plasma membrane protein to an internal membrane pool.
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Citation: J Biol Chem. 1990 Oct 25;265(30):18546-53.
The Journal of biological chemistry
Farwell, Alan P.; Lynch, Ronald M.; Okulicz, William C.; Comi, Ann M.; and Leonard, Jack L., "The actin cytoskeleton mediates the hormonally regulated translocation of type II iodothyronine 5'-deiodinase in astrocytes" (1990). Open Access Articles. 860.