Evidence for the mechanosensor function of filamin in tissue development.
Cells integrate mechanical properties of their surroundings to form multicellular, three-dimensional tissues of appropriate size and spatial organisation. Actin cytoskeleton-linked proteins such as talin, vinculin and filamin function as mechanosensors in cells, but it has yet to be tested whether the mechanosensitivity is important for their function in intact tissues. Here we tested, how filamin mechanosensing contributes to oogenesis in Drosophila. Mutations that require more or less force to open the mechanosensor region demonstrate that filamin mechanosensitivity is important for the maturation of actin-rich ring canals that are essential for Drosophila egg development. The open mutant was more tightly bound to the ring canal structure while the closed mutant dissociated more frequently. Thus, our results show that an appropriate level of mechanical sensitivity is required for filamins' function and dynamics during Drosophila egg growth and support the structure-based model in which the opening and closing of the mechanosensor region regulates filamin binding to cellular components.
Department of Environmental and Biological Science, and Nanoscience Center, University of Jyväskylä, Survontie 9C, FI40014 Jyväskylä, Finland.|Department of Physiology, Development and Neuroscience, and Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Sven
S
Huelsmann
Department of Environmental and Biological Science, and Nanoscience Center, University of Jyväskylä, Survontie 9C, FI40014 Jyväskylä, Finland.
Nina
N
Rintanen
Department of Environmental and Biological Science, and Nanoscience Center, University of Jyväskylä, Survontie 9C, FI40014 Jyväskylä, Finland.
Ritika
R
Sethi
Department of Physiology, Development and Neuroscience, and Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Nicholas H
NH
Brown
Department of Environmental and Biological Science, and Nanoscience Center, University of Jyväskylä, Survontie 9C, FI40014 Jyväskylä, Finland.|Department of Physiology, Development and Neuroscience, and Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Jari
J
Ylänne
D000199:Actins / Q000378:metabolism; D000818:Animals; D004330:Drosophila / Q000378:metabolism; D005260:Female; D064448:Filamins / Q000378:metabolism*; D008297:Male; D009154:Mutation / Q000502:physiology; D009866:Oogenesis / Q000502:physiology; D010063:Ovum / Q000378:metabolism; D011485:Protein Binding; D016608:Talin / Q000378:metabolism; D016596:Vinculin / Q000378:metabolism
D000199:Actins; D064448:Filamins; D016608:Talin; D016596:Vinculin