Extending the molecular clutch beyond actin-based cell motility.
Many cell movements occur via polymerization of the actin cytoskeleton beneath the plasma membrane at the front of the cell, forming a protrusion called a lamellipodium, while myosin contraction squeezes forward the back of the cell. In what is known as the "molecular clutch" description of cell motility, forward movement results from the engagement of the acto-myosin motor with cell-matrix adhesions, thus transmitting force to the substrate and producing movement. However during cell translocation, clutch engagement is not perfect, and as a result, the cytoskeleton slips with respect to the substrate, undergoing backward (retrograde) flow in the direction of the cell body. Retrograde flow is therefore inversely proportional to cell speed and depends on adhesion and acto-myosin dynamics. Here we asked whether the molecular clutch was a general mechanism by measuring motility and retrograde flow for theCaenorhabditis eleganssperm cell in different adhesive conditions. These cells move by adhering to the substrate and emitting a dynamic lamellipodium, but the sperm cell does not contain an acto-myosin cytoskeleton. Instead the lamellipodium is formed by the assembly of Major Sperm Protein (MSP), which has no biochemical or structural similarity to actin. We find that these cells display the same molecular clutch characteristics as acto-myosin containing cells. We further show that retrograde flow is produced both by cytoskeletal assembly and contractility in these cells. Overall this study shows that the molecular clutch hypothesis of how polymerization is transduced into motility via adhesions is a general description of cell movement regardless of the composition of the cytoskeleton.
Institut Curie, Centre de Recherche, Paris, F-75248 France ; Centre National de la Recherche Scientifique, Unité Mixte de Recherche 168, Paris, F-75248 France ; Université Pierre et Marie Curie, Paris F-75248, France.
Svitlana
S
Havrylenko
Institut Curie, Centre de Recherche, Paris, F-75248 France ; Centre National de la Recherche Scientifique, Unité Mixte de Recherche 168, Paris, F-75248 France ; Université Pierre et Marie Curie, Paris F-75248, France.
Xavier
X
Mezanges
Institut Curie, Centre de Recherche, Paris, F-75248 France ; Centre National de la Recherche Scientifique, Unité Mixte de Recherche 168, Paris, F-75248 France ; Université Pierre et Marie Curie, Paris F-75248, France.
Ellen
E
Batchelder
Institut Curie, Centre de Recherche, Paris, F-75248 France ; Centre National de la Recherche Scientifique, Unité Mixte de Recherche 168, Paris, F-75248 France ; Université Pierre et Marie Curie, Paris F-75248, France.
Julie
J
Plastino