TY - JOUR
T1 - Mechanical role of actin dynamics in the rheology of the Golgi complex and in Golgi-associated trafficking events
AU - Guet, David
AU - Mandal, Kalpana
AU - Pinot, Mathieu
AU - Hoffmann, Jessica
AU - Abidine, Yara
AU - Sigaut, Walter
AU - Bardin, Sabine
AU - Schauer, Kristine
AU - Goud, Bruno
AU - Manneville, Jean Baptiste
N1 - Funding Information:
We thank Patricia Bassereau, Benoît Sorre, Aurélien Roux, Gil Toombes, and Xavier Mezanges for assistance in the design of the experimental set-up. We thank Rob Phillips, Pierre Sens, Bruno Antonny, Cathy Jackson, Samuel Bouvet, Jean Salamero, Catherine Dargemont, Stéphanie Miserey-Lenkei, and Giovanni Capello for stimulating discussions. This work was in part performed within the Nikon Imaging Center @ Institut Curie. Assistance from the BioImaging Cell and Tissue Core Facility of the Institut Curie (PICT-IBiSA) is acknowledged. D.G. is funded by a grant from the French Ministry of Research. Other funding is from Institut Curie, CNRS (Program “Prise de risque à l’interface Physique-Biologie”), ANR (grant number ANR09-JCJC-0020-01), and INSERM Plan Cancer 2009-2013 INSERM - CEA Tecsan (grant number PC201125).
PY - 2014/8/4
Y1 - 2014/8/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84905656743&partnerID=8YFLogxK
U2 - 10.1016/j.cub.2014.06.048
DO - 10.1016/j.cub.2014.06.048
M3 - Article
C2 - 25042587
AN - SCOPUS:84905656743
SN - 0960-9822
VL - 24
SP - 1700
EP - 1711
JO - Current Biology
JF - Current Biology
IS - 15
ER -