Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila

ELife
Hannah J GreenNicholas H Brown

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.

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Citations

Jul 18, 2019·Physiological Reviews·Michael BachmannBernhard Wehrle-Haller
May 13, 2020·Journal of Cell Science·Nuria Barber-PérezJohanna Ivaska
Jun 26, 2020·The Journal of Cell Biology·Megan R ChastneyMartin J Humphries
Aug 25, 2019·Essays in Biochemistry·James R W Conway, Guillaume Jacquemet
Jul 8, 2020·Cells·Preethi Poovathumkadavil, Krzysztof Jagla
Dec 3, 2020·Molecular Biology Reports·Madhavi DubeyHena Firdaus
Aug 28, 2021·BMC Developmental Biology·Antonio Celestino-MontesFidel de la Cruz Hernández-Hernández

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Methods Mentioned

BETA
electron microscopy
confocal microscopy
transgenic
transmission electron microscopy
super-resolution
PCR
fluorescence microscopy

Software Mentioned

Excel
Matlab
Prism
GraphPad
ImageJ
softWoRx

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