Relevance of dopamine signals anchoring dynamin-2 to the plasma membrane during Na+,K+-ATPase endocytosis.
Enviado por Guillermo Yudowski el
Título | Relevance of dopamine signals anchoring dynamin-2 to the plasma membrane during Na+,K+-ATPase endocytosis. |
Publication Type | Journal Article |
Year of Publication | 2002 |
Autores | Efendiev, R, Yudowski, GA, Zwiller, J, Leibiger, B, Katz, AI, Berggren, P-O, Pedemonte, CH, Leibiger, IB, Bertorello, AM |
Journal | J Biol Chem |
Volume | 277 |
Issue | 46 |
Pagination | 44108-14 |
Date Published | 2002 Nov 15 |
ISSN | 0021-9258 |
Palabras clave | Animals, Blotting, Western, Cell Line, Cell Membrane, Cells, Cultured, Clathrin, Dopamine, Dynamin II, Dynamins, Electrophoresis, Polyacrylamide Gel, Endocytosis, Green Fluorescent Proteins, Kinetics, Luminescent Proteins, Microscopy, Confocal, Models, Biological, Phosphatidylinositol 3-Kinases, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Rats, Sodium-Potassium-Exchanging ATPase, Time Factors, Transfection |
Abstract | Clathrin-dependent endocytosis of Na(+),K(+)-ATPase in response to dopamine regulates its catalytic activity in intact cells. Because fission of clathrin-coated pits requires dynamin, we examined the mechanisms by which dopamine receptor signals promote dynamin-2 recruitment and assembly at the site of Na(+),K(+)-ATPase endocytosis. Western blotting revealed that dopamine increased the association of dynamin-2 with the plasma membrane and with phosphatidylinositol 3-kinase. Dopamine inhibited Na(+),K(+)-ATPase activity in OK cells and in those overexpressing wild type dynamin-2 but not in cells expressing a dominant-negative mutant. Dephosphorylation of dynamin is important for its assembly. Dopamine increased protein phosphatase 2A activity and dephosphorylated dynamin-2. In cells expressing a dominant-negative mutant of protein phosphatase 2A, dopamine failed to dephosphorylate dynamin-2 and to reduce Na(+),K(+)-ATPase activity. Dynamin-2 is phosphorylated at Ser(848), and expression of the S848A mutant significantly blocked the inhibitory effect of dopamine. These results demonstrate a distinct signaling network originating from the dopamine receptor that regulates the state of dynamin-2 phosphorylation and that promotes its location (by interaction with phosphatidylinositol 3-kinase) at the site of Na(+),K(+)-ATPase endocytosis. |
DOI | 10.1074/jbc.M205173200 |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 12205083 |
Grant List | DK 53460 / DK / NIDDK NIH HHS / United States |