Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2

Shaun G. Weller, Mirco Capitani, Hong Cao, Massimo Micaroni, Alberto Luini, Michele Sallese, Mark A. McNiven

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


The size and integrity of the Golgi apparatus is maintained via a tightly controlled regulation of membrane traffic using a variety of different signaling and cytoskeletal proteins. We have recently observed that activation of c-Src has profound effects on Golgi structure, leadingto dramatically vesiculatedcisternae in a variety of cell types. As the large GTPase dynamin (Dyn2) has been implicated in Golgi vesiculation during secretion, we tested whether inhibiting Dyn2 activity by expression of a Dyn2K44A mutant or siRNA knockdown could attenuate active Src-induced Golgi fragmentation. Indeed, these perturbations attenuated fragmentation, and expression of a Dyn2Y(231/597)F mutant protein that cannot be phosphorylated by Src kinase had a similar effect . Finally, we find that Dyn2 is markedly phosphorylated during the transit of VSV-G protein through the TGNwhereas expression of the Dyn2Y(231/597) F mutant significantly reduces exit of the nascent protein from this compartment. These findings demonstrate that activation of Dyn2 by Src kinase regulates Golgi integrity and vesiculation during the secretory process.

Original languageEnglish (US)
Pages (from-to)5863-5868
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
StatePublished - Mar 30 2010


  • Dynamin
  • Golgi vesiculation

ASJC Scopus subject areas

  • General


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