Dynamin-actin cross-talk contributes to phagosome formation and closure

Florence Marie-Anaïs, Julie Mazzolini, Floriane Herit, Florence Niedergang

Research output: Contribution to journalArticlepeer-review

Abstract

Phagocytosis is a mechanism used by macrophages to internalize and eliminate microorganisms or cellular debris. It relies on profound rearrangements of the actin cytoskeleton that is the driving force allowing plasma membrane extension around the particle. The closure step of phagocytosis, however, remains poorly defined. We used a dedicated experimental set up with Total Internal Reflection Fluorescence Microscopy (TIRFM) to monitor phagosome formation and closure in three dimensions in living cells. We show that dynamin-2, which mediates the scission of endocytic vesicles, was recruited early and concomitantly with actin during phagosome formation. Dynamin-2 accumulated at the site of phagosome closure in living macrophages. Inhibition of its activity with dominant negative mutants or drugs demonstrated that dynamin-2 is implicated in actin dynamics and pseudopod extension. Depolymerization of actin led to impaired dynamin-2 recruitment or activity. Finally, we show that dynamin-2 plays a critical role in the effective scission of the phagosome from the plasma membrane. Thus, we establish that a crosstalk between actin and dynamin takes place for phagosome formation and closure before dynamin functions for scission.

Original languageEnglish
JournalTraffic
Early online date5 Feb 2016
DOIs
Publication statusPublished - May 2016

Fingerprint

Dive into the research topics of 'Dynamin-actin cross-talk contributes to phagosome formation and closure'. Together they form a unique fingerprint.

Cite this