Myosin 1b functions as an effector of EphB signaling to control cell repulsion

Journal of Cell Biology - Tập 210 Số 2 - Trang 347-361 - 2015
Marie‐Thérèse Prosperi1, Priscilla Lépine1,2, Florent Dingli3, Perrine Paul‐Gilloteaux4,1, René Martin5, Damarys Loew3, Hans‐Joachim Knölker5, Evelyne Coudrier4,1
1Institut Curie, Centre de Recherche, F-75248 Paris, France 1
2Université Pierre et Marie Curie, F-75252 Paris, France 3
3Laboratoire de Spectrométrie de Masse Protéomique, Institut Curie, Centre de Recherche, F-75248 Paris, France 2
4Cell and Tissue Imaging Facility (PICT-IBiSA), Centre National de la Recherche Scientifique, UMR 144, Paris F-75248, France 4
5Department of Chemistry, Technische Univesität, 01069 Dresden, Germany 5

Tóm tắt

Eph receptors and their membrane-tethered ligands, the ephrins, have important functions in embryo morphogenesis and in adult tissue homeostasis. Eph/ephrin signaling is essential for cell segregation and cell repulsion. This process is accompanied by morphological changes and actin remodeling that drives cell segregation and tissue patterning. The actin cortex must be mechanically coupled to the plasma membrane to orchestrate the cell morphology changes. Here, we demonstrate that myosin 1b that can mechanically link the membrane to the actin cytoskeleton interacts with EphB2 receptors via its tail and is tyrosine phosphorylated on its tail in an EphB2-dependent manner. Myosin 1b regulates the redistribution of myosin II in actomyosin fibers and the formation of filopodia at the interface of ephrinB1 and EphB2 cells, which are two processes mediated by EphB2 signaling that contribute to cell repulsion. Together, our results provide the first evidence that a myosin 1 functions as an effector of EphB2/ephrinB signaling, controls cell morphology, and thereby cell repulsion.

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