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Zipper Nonmuscle Myosin-II Functions Downstream of PS2 Integrin during Drosophila Myogenesis and is necessary for Myofibril Formation

Bloor, James W., Kiehart, Daniel P. (2001) Zipper Nonmuscle Myosin-II Functions Downstream of PS2 Integrin during Drosophila Myogenesis and is necessary for Myofibril Formation. Developmental Biology, 239 (2). pp. 215-228. ISSN 0012-1606. (doi:10.1006/dbio.2001.0452) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:9892)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1006/dbio.2001.0452

Abstract

Nonmuscle myosin-II is a key motor protein that drives cell shape change and cell movement. Here, we analyze the function of nonmuscle myosin-II during Drosophila embryonic myogenesis. We find that nonmuscle myosin-II and the adhesion molecule, PS2 integrin, colocalize at the developing muscle termini. In the paradigm emerging from cultured fibroblasts, nonmuscle actomyosin-II contractility, mediated by the small GTPase Rho, is required to cluster integrins at focal adhesions. In direct opposition to this model, we find that neither nonmuscle myosin-II nor RhoA appear to function in PS2 clustering. Instead, PS2 integrin is required for the maintenance of nonmuscle myosin-II localization and we show that the cytoplasmic tail of the ?PS integrin subunit is capable of mediating this PS2 integrin function. We show that embryos that lack zygotic expression of nonmuscle myosin-II fail to form striated myofibrils. In keeping with this, we demonstrate that a PS2 mutant that specifically disrupts myofibril formation is unable to mediate proper localization of nonmuscle myosin-II at the muscle termini. In contrast, embryos that lack RhoA function do generate striated muscles. Finally, we find that nonmuscle myosin-II localizes to the Z-line in mature larval muscle. We suggest that nonmuscle myosin-II functions at the muscle termini and the Z-line as an actin crosslinker and acts to maintain the structural integrity of the sarcomere.

Item Type: Article
DOI/Identification number: 10.1006/dbio.2001.0452
Subjects: Q Science > QH Natural history > QH426 Genetics
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: James Bloor
Date Deposited: 17 Mar 2009 11:19 UTC
Last Modified: 16 Nov 2021 09:48 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/9892 (The current URI for this page, for reference purposes)

University of Kent Author Information

Bloor, James W..

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