Dynamin 2 is required for phagocytosis in macrophages

Elizabeth S. Gold, David M. Underhill, Naomi S. Morrissette, Jian Guo, Mark A. McNiven, Alan Aderem

Research output: Contribution to journalArticlepeer-review

212 Scopus citations


Cells internalize soluble ligands through endocytosis and large particles through actin-based phagocytosis. The dynamin family of GTPases mediates the scission of endocytic vesicles from the plasma membrane. We report here that dynamin 2, a ubiquitously expressed dynamin isoform, has a role in phagocytosis in macrophages. Dynamin 2 is enriched on early phagosomes, and expression of a dominant-negative mutant of dynamin 2 significantly inhibits particle internalization at the stage of membrane extension around the particle. This arrest in phagocytosis resembles that seen with inhibitors of phosphoinositide 3-kinase (PI3K), and inhibition of PI3K prevents the recruitment of dynamin to the site of particle binding. Although expression of mutant dynamin in macrophages inhibited particle internalization, it had no effect on the production of inflammatory mediators elicited by particle binding.

Original languageEnglish (US)
Pages (from-to)1849-1856
Number of pages8
JournalJournal of Experimental Medicine
Issue number12
StatePublished - Dec 20 1999


  • Dynamin
  • Inflammation
  • Macrophages
  • Phagocytosis
  • Phosphoinositide 3-kinase

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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