Apical spectrin organizes cortical actin filament bundles to pattern C. elegans cuticle ridges.

Authors

Prioty Ferheen Sarwar, Trevor James Barker, Ken Nguyen, Fung-Yi Chan, David H Hall, Ana Xavier Carvalho, Meera Vedavalli Sundaram

Published in

PLoS genetics. Volume 22. Issue 7. Pages e1012236. Jul 16, 2026. Epub Jul 16, 2026.

Abstract

The apical extracellular matrix can form elaborate three-dimensional structures on animal surfaces. To better understand the mechanisms that pattern and shape these structures, we focus on development of collagen-rich cuticle ridges (alae) in adult C. elegans. Previous studies suggested that longitudinal actin filament bundles (AFBs) in the lateral seam epidermis specify alae position through a mechanism that involves post-secretory matrix delamination. Here we identify additional components of this highly organized cortical actin network and show that loss of the apical βH-spectrin SMA-1 specifically disrupts organization of the two AFBs that would normally flank the site where the middle alae ridge forms. Correspondingly, sma-1 loss, or mutation of its actin binding domains, also disrupts formation of the middle alae ridge. Ultrastructurally, sma-1 mutants have expanded regions of matrix delamination that can explain middle ridge loss. Together, these data highlight the importance of apical spectrin for organizing a patterned actin network within epithelia and show that, via its effects on actin organization, spectrin can also change the extracellular matrix and its patterns on animal surfaces.

PMID:
42461972
Bibliographic data and abstract were imported from PubMed on 17 Jul 2026.

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