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Molnar, K.

Publications and source records attributed to Molnar, K..

2 recordsLinked to original sources

Repeated extrinsic and anisotropic mechanical inputs promote polarized adherens junction elongation

A key challenge in development is understanding how complex organisms physically coordinate the morphogenesis of multiple tissues. Here, using biophysical approaches, we investigate how muscles under the epidermis specifically stimulate the extension of anterior-posterior (AP-oriented) epidermal adherens junctions during late C. elegans embryonic elongation. First, light-sheet imaging shows that asynchronous patterns of muscle contractions drive embryo rotations. In turn, junctions between the lateral and dorso-ventral epidermis repeatedly oscillate between a folded, hypotensed state, and an extended, hypertensed state. Second, FRAP (Fluorescence Recovery After Photobleaching) analysis of an E-cadherin::GFP construct shows that muscle contractions stimulate E-cadherin turnover. Moreover, a mechano-chemical model backed by genetic tests suggests that E-cadherin trafficking modulates junction elongation due to lower line tension. Altogether, our results illustrate how muscle contractions fluidize epidermal adherens junctions, which, combined with anisotropic tension in the epidermis, drives their polarized extension.

developmental biology↗

Conditional nmy-1 and nmy-2 alleles establish that non-muscle myosins are required for late C. elegans embryonic elongation

The elongation of C. elegans embryos allows examination of mechanical interactions between adjacent tissues. Muscle contractions during late elongation induce the remodelling of epidermal circumferential actin filaments through mechanotransduction. We investigated the possible role of the non-muscle myosins NMY-1 and NMY-2 in this process using nmy-1 and nmy-2 thermosensitive alleles. Our findings suggest these myosins act redundantly in late elongation, and that they are involved in the multi-step process of epidermal remodeling. When inactivated, NMY-1 was seen to form protein aggregates.

developmental biology↗