Molecular Biology of the CellCell BiologyPeer-reviewed journal article
Linear Z-line-like alignment of capping protein in obliquely striated muscle of the nematode C. elegans suggests that dense bodies are not equivalent to Z-lines
Shoichiro OnoiD, Emily Nickoloff-Bybel, Kennosuke Kurimaru, Kanako Ono
Abstract
Many invertebrates have obliquely striated muscles, in which neighboring thin and thick filaments are staggered and aligned in an oblique manner. This type of muscle allows force production over a wide range of lengths and is beneficial for soft-bodied animals. Unlike cross-striated muscles of vertebrates, most of obliquely striated muscles lack distinct Z-lines and, instead, have dense bodies. Because the dense bodies are located in the middle of the I-bands and contain -actinin, the dogma is that dense bodies are equivalent to the Z-lines anchoring the actin barbed ends. However, we present evidence that the barbed ends of sarcomeric actin filaments in the nematode Caenorhabditis elegans body wall muscle are aligned in a linear Z-line-like arrangement without converging at the dense bodies. Colocalization of F-actin and ATN-1/-actinin was minimal. Furthermore, CAP-1, an -subunit of capping protein/CapZ, was linearly aligned in the middle of the I-bands without concentration at the dense bodies. This linear CAP-1 alignment was maintained in the absence of ATN-1. These results demonstrate that the actin barbed ends are not directly anchored to the dense bodies. Depletion of the capping protein subunit, CAP-1 or CAP-2, caused embryonic or larval lethality with severe actin disorganization in the body wall muscle, indicating that barbed-end regulation by capping protein is essential for sarcomere assembly. These results contradict the current view of the sarcomere organization in C. elegans muscle and suggest a new model of a linear Z-line-like arrangement of actin barbed ends. Significance StatementO_LIWithout clear evidence, there has been a notion that actin filaments are directly anchored to the dense bodies in C. elegans striated muscle. C_LIO_LICapping protein localizes in a linear Z-line-like alignment in C. elegans muscle without concentrating at the dense bodies, indicating that the actin barbed ends are not directly anchored at the dense bodies. C_LIO_LIDepletion of capping protein causes severe sarcomere defects in embryos and larvae indicating a critical role of capping protein in sarcomere assembly. C_LI
- organism: C. elegans
- assay: proteomics
- research focus: cell type annotation
- research focus: cell signaling & trafficking
- research focus: development & morphogenesis
- approach: experimental assay
- approach: genetic perturbation / CRISPR
- Citations
- 0
- FWCI
- 0.00
- Field percentile
- 11th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Investigating the correlation of muscle function tests and sarcomere organization in C. elegans
L. Lesanpezeshki, H. Qadota, … S. A. Vanapalli·bioRxiv·Apr 13, 2021
- Activity-dependent remodeling of muscle architecture during distinct locomotor behaviors in Caenorhabditis elegans
Adina Fazyl, A Anbu, … Andres Gabriel Vidal-Gadea·Biology OpenPeer-reviewed·Dec 23, 2025
- FHOD-1/profilin-mediated actin assembly protects sarcomeres against contraction-induced deformation in C. elegans
M. J. Kimmich, S. Sundaramurthy, … D. Pruyne·bioRxiv·Feb 29, 2024
- Actin capping protein regulates actomyosin contractility to maintain germline architecture in C. elegans
S. Ray, P. Agarwal, R. Zaidel-Bar·bioRxiv·Oct 3, 2021
- Capping protein regulates the balance of assembly among diverse actin networks in C. elegans zygotes
Sarah E. Yde, Cristian Suarez, … David R. Kovar·bioRxiv·Mar 24, 2026
- FHOD-1 is the only formin in Caenorhabditis elegans that promotes striated muscle growth and Z-line organization in a cell autonomous manner
Sumana Sundaramurthy, SarahBeth D. Votra, … David Pruyne·CytoskeletonPeer-reviewed·Oct 1, 2020