Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila.
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Publication Date
2018-07-20Journal Title
Elife
ISSN
2050-084X
Publisher
eLife Sciences Publications, Ltd
Volume
7
Language
eng
Type
Article
Physical Medium
Electronic
Metadata
Show full item recordCitation
Green, H. J., Griffiths, A. G., Ylänne, J., & Brown, N. H. (2018). Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila.. Elife, 7 https://doi.org/10.7554/eLife.35783
Abstract
We use the myotendinous junction of Drosophila flight muscles to explore why many integrin associated proteins (IAPs) are needed and how their function is coordinated. These muscles revealed new functions for IAPs not required for viability: Focal Adhesion Kinase (FAK), RSU1, tensin and vinculin. Genetic interactions demonstrated a balance between positive and negative activities, with vinculin and tensin positively regulating adhesion, while FAK inhibits elevation of integrin activity by tensin, and RSU1 keeps PINCH activity in check. The molecular composition of myofibril termini resolves into 4 distinct layers, one of which is built by a mechanotransduction cascade: vinculin facilitates mechanical opening of filamin, which works with the Arp2/3 activator WASH to build an actin-rich layer positioned between integrins and the first sarcomere. Thus, integration of IAP activity is needed to build the complex architecture of the myotendinous junction, linking the membrane anchor to the sarcomere.
Keywords
Muscles, Myofibrils, Sarcomeres, Animals, Drosophila melanogaster, Actins, Vinculin, Drosophila Proteins, Integrins, Epistasis, Genetic, RNA Interference, Flight, Animal, Phenotype, Mutation
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/L006669/1)
Wellcome Trust (099739/Z/12/Z)
Identifiers
External DOI: https://doi.org/10.7554/eLife.35783
This record's URL: https://www.repository.cam.ac.uk/handle/1810/284569
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