A1 Journal article (refereed)
Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila (2018)

Green, H. J., Griffiths, A. G. M., Ylänne, J., & Brown, N. H. (2018). Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila. eLife, 7, Article e35783. https://doi.org/10.7554/eLife.35783

JYU authors or editors

Ylänne, Jari

Publication details

All authors or editors: Green, Hannah J.; Griffiths, Annabel G. M.; Ylänne, Jari; Brown, Nicholas H.

Journal or series: eLife

ISSN: 2050-084X

eISSN: 2050-084X

Publication year: 2018

Volume: 7

Issue number: 0

Article number: e35783

Publisher: eLife Sciences Publications

Publication country: United Kingdom

Publication language: English

DOI: https://doi.org/10.7554/eLife.35783

Publication open access: Openly available

Publication channel open access: Open Access channel

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: muscle cells; cell membranes; integrins; proteins; Drosophila melanogaster