Mechanical role of actin dynamics in the rheology of the Golgi complex and in Golgi-associated trafficking events

Curr Biol. 2014 Aug 4;24(15):1700-11. doi: 10.1016/j.cub.2014.06.048. Epub 2014 Jul 17.

Abstract

Background: In vitro studies have shown that physical parameters, such as membrane curvature, tension, and composition, influence the budding and fission of transport intermediates. Endocytosis in living cells also appears to be regulated by the mechanical load experienced by the plasma membrane. In contrast, how these parameters affect intracellular membrane trafficking in living cells is not known. To address this question, we investigate here the impact of a mechanical stress on the organization of the Golgi complex and on the formation of transport intermediates from the Golgi complex.

Results: Using confocal microscopy, we visualize the deformation of Rab6-positive Golgi membranes applied by an internalized microsphere trapped in optical tweezers and simultaneously measure the corresponding forces. Our results show that the force necessary to deform Golgi membranes drops when actin dynamics is altered and correlates with myosin II activity. We also show that the applied stress has a long-range effect on Golgi membranes, perturbs the dynamics of Golgi-associated actin, and induces a sharp decrease in the formation of Rab6-positive vesicles from the Golgi complex as well as tubulation of Golgi membranes.

Conclusions: We suggest that acto-myosin contractility strongly contributes to the local rigidity of the Golgi complex and regulates the mechanics of the Golgi complex to control intracellular membrane trafficking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Biomechanical Phenomena
  • Cells, Cultured
  • Golgi Apparatus / metabolism*
  • Humans
  • Intracellular Membranes / metabolism*
  • Microscopy, Confocal
  • Myosin Type II / metabolism
  • Rheology
  • rab GTP-Binding Proteins / metabolism

Substances

  • Actins
  • Rab6 protein
  • Myosin Type II
  • rab GTP-Binding Proteins