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Integrin signaling downregulates filopodia in muscle-tendon attachment

View ORCID ProfileBenjamin Richier, Yoshiko Inoue, View ORCID ProfileUlrich Dobramysl, Jonathan Friedlander, Nicholas H. Brown, View ORCID ProfileJennifer L. Gallop
doi: https://doi.org/10.1101/270546
Benjamin Richier
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
2Dept. of Biochemistry, University of Cambridge
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Yoshiko Inoue
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
2Dept. of Biochemistry, University of Cambridge
3Dept. of Physiology, Development and Neuroscience, University of Cambridge
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Ulrich Dobramysl
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
2Dept. of Biochemistry, University of Cambridge
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Jonathan Friedlander
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
3Dept. of Physiology, Development and Neuroscience, University of Cambridge
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Nicholas H. Brown
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
3Dept. of Physiology, Development and Neuroscience, University of Cambridge
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Jennifer L. Gallop
1The Gurdon Institute, Tennis Court Rd, Cambridge CB2 1QN, United Kingdom
2Dept. of Biochemistry, University of Cambridge
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  • For correspondence: j.gallop@gurdon.cam.ac.uk
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Abstract

Cells in developing tissues need to sense their environment for their accurate targeting to specific destinations. This occurs in developing muscles, which need to attach to their respective tendon cell before muscle contractions can begin. Elongating myotube tips form filopodia, which are presumed to have sensory roles, and are later suppressed upon building the attachment site. Here, we use live imaging and quantitative image analysis of lateral transverse (LT) myotubes in Drosophila to show that filopodia suppression occurs as a result of integrin signaling. Loss of the integrin subunits αPS2 and βPS increased filopodia number and length at stages when they are normally suppressed. Conversely, inducing integrin signaling, achieved by expression of constitutively dimerised βPS cytoplasmic domain (diβ), prematurely suppressed filopodia. We discovered that the integrin signal is transmitted through the ArfGAP and scaffolding protein Git (G-protein receptor coupled interacting protein) and its downstream kinase Pak (p21-activated kinase). Absence of these proteins causes profuse filopodia formation and prevents filopodial inhibition by diβ. Thus, integrin signaling switches off the exploratory behaviour of myotubes seeking tendons, enabling the actin machinery to focus on forming a strong attachment and assembling the contractile apparatus.

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  • ↵* Joint first authors

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Posted February 23, 2018.
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Integrin signaling downregulates filopodia in muscle-tendon attachment
Benjamin Richier, Yoshiko Inoue, Ulrich Dobramysl, Jonathan Friedlander, Nicholas H. Brown, Jennifer L. Gallop
bioRxiv 270546; doi: https://doi.org/10.1101/270546
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Integrin signaling downregulates filopodia in muscle-tendon attachment
Benjamin Richier, Yoshiko Inoue, Ulrich Dobramysl, Jonathan Friedlander, Nicholas H. Brown, Jennifer L. Gallop
bioRxiv 270546; doi: https://doi.org/10.1101/270546

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