zipper Nonmuscle myosin-II functions downstream of PS2 integrin in Drosophila myogenesis and is necessary for myofibril formation.

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 beta(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.

journal_name

Dev Biol

journal_title

Developmental biology

authors

Bloor JW,Kiehart DP

doi

10.1006/dbio.2001.0452

subject

Has Abstract

pub_date

2001-11-15 00:00:00

pages

215-28

issue

2

eissn

0012-1606

issn

1095-564X

pii

S0012-1606(01)90452-X

journal_volume

239

pub_type

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