A glutamate receptor-interacting protein homolog organizes muscle guidance in Drosophila

• Published in: Genes & development Vol. 18; no. 2; pp. 223 - 237
• Main Authors: Swan, Laura E, Wichmann, Carolin, Prange, Ulrike, Schmid, Andreas, Schmidt, Manuela, Schwarz, Tobias, Ponimaskin, Evgeni, Madeo, Frank, Vorbrüggen, Gerd, Sigrist, Stephan J
• Format: Journal Article
• Language: English
• Published: United States Cold Spring Harbor Laboratory Press 15.01.2004
• Subjects: Animals; Carrier Proteins - metabolism; Cell Differentiation - physiology; Drosophila; Drosophila - embryology; Drosophila - metabolism; Drosophila Proteins; glutamate receptor interacting protein; grip gene; Muscles - abnormalities; Muscles - embryology; Muscles - metabolism; Nerve Tissue Proteins - metabolism; Receptors, AMPA - metabolism; Research Papers
• ISSN: 0890-9369; 1549-5477
• DOI: 10.1101/gad.287604

During Drosophila embryogenesis, developing muscles extend growth-cone-like structures to navigate toward specific epidermal attachment sites. Here, we show that the homolog of Glutamate Receptor-Interacting Proteins (DGrip) acts as a key component of proper muscle guidance. Mutations in dgrip impair patterning of ventral longitudinal muscles (VLMs), whereas lateral transverse muscles (LTMs) that attach to intrasegmental attachment sites develop normally. Myoblast fusion, stabilization of muscle contacts, and general muscle function are not impaired in the absence of DGrip. Instead, the proper formation of cellular extensions during guidance fails in dgrip mutant VLMs. DGrip protein concentrates at the ends of VLMs while these muscles guide toward segment border attachment sites. Conversely, LTMs overexpressing DGrip form ectopic cellular extensions that can cause attachment of these muscles to other muscles at segment borders. Our data suggest that DGrip participates in the reception of an attractive signal that emanates from the epidermal attachment sites to direct the motility of developing muscles. This dgrip phenotype should be valuable to study mechanistic principles of Grip function.