Relevance of dopamine signals anchoring dynamin-2 to the plasma membrane during Na+,K+-ATPase endocytosis

Riad Efendiev, Guillermo A. Yudowski, Jean Zwiller, Barbara Leibiger, Adrian I. Katz, Per Olof Berggren, Carlos H. Pedemonte, Ingo B. Leibiger, Alejandro M. Bertorello

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


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 Ser848, 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.

Original languageEnglish (US)
Pages (from-to)44108-44114
Number of pages7
JournalJournal of Biological Chemistry
Issue number46
StatePublished - Nov 15 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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