Notochord segmentation in zebrafish controlled by iterative mechanical signaling.
Date
2024-07
Journal Title
Journal ISSN
Volume Title
Repository Usage Stats
views
downloads
Citation Stats
Attention Stats
Abstract
In bony fishes, patterning of the vertebral column, or spine, is guided by a metameric blueprint established in the notochord sheath. Notochord segmentation begins days after somitogenesis concludes and can occur in its absence. However, somite patterning defects lead to imprecise notochord segmentation, suggesting that these processes are linked. Here, we identify that interactions between the notochord and the axial musculature ensure precise spatiotemporal segmentation of the zebrafish spine. We demonstrate that myoseptum-notochord linkages drive notochord segment initiation by locally deforming the notochord extracellular matrix and recruiting focal adhesion machinery at these contact points. Irregular somite patterning alters this mechanical signaling, causing non-sequential and dysmorphic notochord segmentation, leading to altered spine development. Using a model that captures myoseptum-notochord interactions, we find that a fixed spatial interval is critical for driving sequential segment initiation. Thus, mechanical coupling of axial tissues facilitates spatiotemporal spine patterning.
Type
Department
Description
Provenance
Subjects
Citation
Permalink
Published Version (Please cite this version)
Publication Info
Wopat, Susan, Priyom Adhyapok, Bijoy Daga, Janice M Crawford, James Norman, Jennifer Bagwell, Brianna Peskin, Indrasen Magre, et al. (2024). Notochord segmentation in zebrafish controlled by iterative mechanical signaling. Developmental cell, 59(14). pp. 1860–1875.e5. 10.1016/j.devcel.2024.04.013 Retrieved from https://hdl.handle.net/10161/32196.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
Collections
Scholars@Duke
Daniel Levic
Stefano Di Talia
Daniel P. Kiehart
Our intellectual focus is on identifying determinants of cell shape that function during development. Utilizing molecular genetic and reverse genetic approaches in Drosophila, we have shown that conventional nonmuscle myosin is necessary for driving both cell division and post-mitotic cell shape changes for morphogenesis. Currently, we are investigating how myosin elicits cell shape change and how its function is regulated through filament formation, phosphorylation, sub-cellular targeting, small GTP-binding proteins, kinase and phosphatase functions. In fly, we are using novel, near saturating screens to identify mutations that perturb dorsal closure, a model cell sheet movement that requires at least six different filamentous actin and/or actomyosin arrays for proper morphogenesis. Our screens show that nearly all aspects of closure a mutable -- by extrapolating our results, which have thus far screened approximately two-fifths of the fly genome, we project that the function of over 300 genes are required to drive this superficially simple, yet remarkably complex and sophisticated morphogenic process. We have also identified gene products that are necessary for myosin function by genetically recovering second site non-complementing loci and biochemically recovering proteins that bind to myosin. To date, our experiments identify ~30 loci that genetically interact with myosin and a kinase activity that phosphorylates myosin heavy chain and establish genetically, that the Rho signalling pathway is required in concert with nonmuscle myosin II for morphogenesis. Finally, we are using laser microsurgery and micro-manipulation studies to understand the forces that drive morphogenesis. We show that both the amnioserosa and the leading edge of the lateral epidermis contribute to the movements of dorsal closure. Finally, we are examining the role these proteins play in movements that occur during wound healing.
Patrick Charbonneau
Professor Charbonneau studies soft matter. His work combines theory and simulation to understand the glass problem, protein crystallization, microphase formation, and colloidal assembly in external fields.
Michel Bagnat
Unless otherwise indicated, scholarly articles published by Duke faculty members are made available here with a CC-BY-NC (Creative Commons Attribution Non-Commercial) license, as enabled by the Duke Open Access Policy. If you wish to use the materials in ways not already permitted under CC-BY-NC, please consult the copyright owner. Other materials are made available here through the author’s grant of a non-exclusive license to make their work openly accessible.