期刊
JOURNAL OF CELL SCIENCE
卷 131, 期 16, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.217133
关键词
Filopodia; Integrin signaling; Actin dynamics; Muscle; Drosophila
类别
资金
- Wellcome Trust [069943, 086451, 092096]
- European Research Council [281971]
- Wellcome Trust Research Career Development Fellowship [WT095829AIA]
- Cancer Research UK [C6946/A14492]
- Junior Interdisciplinary Fellowship (Wellcome Trust grant) [105602/Z/14/Z]
- Junior Interdisciplinary Fellowship (Herchel Smith Postdoctoral Fellowship)
- European Research Council (ERC) [281971] Funding Source: European Research Council (ERC)
Cells need to sense their environment to ensure accurate targeting to specific destinations. This occurs in developing muscles, which need to attach to tendon cells 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 alpha PS2 and beta PS (also known as If and Mys, respectively, in flies) increased filopodia number and length at stages when they are normally suppressed. Conversely, inducing integrin signaling, achieved by the expression of constitutively dimerised beta PS cytoplasmic domain (di beta), prematurely suppressed filopodia. We discovered that the integrin signal is transmitted through the protein G protein-coupled receptor kinase interacting ArfGAP (Git) and its downstream kinase p21-activated kinase (Pak). Absence of these proteins causes profuse filopodia and prevents the filopodial inhibition mediated by di beta. Thus, integrin signaling terminates the exploratory behavior of myotubes seeking tendons, enabling the actin machinery to focus on forming a strong attachment and assembling the contractile apparatus.
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