ArticleDevelopment (Cambridge, England)2024
C. elegans epicuticlins define specific compartments in the apical extracellular matrix and function in wound repair.
Article in Development (Cambridge, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Roles and regulation of the Kunitz domain protein MLT-11 during C. elegans cuticle synthesis and molting.Genetics · 2026Article
- From nematode to Nobel: How community-shared resources fueled the rise ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- MLT-11 is necessary forbioRxiv : the preprint server for biology · 2025Article
- Multiscale patterning of a model apical extracellular matrix revealed by systematic endogenous protein tagging.bioRxiv : the preprint server for biology · 2025Article
- Calcium-binding protein CALU-1 is essential for proper collagen formation in Caenorhabditis elegans.Cellular and molecular life sciences : CMLS · 2025Article
- The Caenorhabditis elegans cuticle and precuticle: a model for studying dynamic apical extracellular matrices in vivo.Genetics · 2024Review
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Abstract
The apical extracellular matrix (aECM) of external epithelia often contains lipid-rich outer layers that contribute to permeability barrier function. The external aECM of nematodes is known as the cuticle and contains an external lipid-rich layer - the epicuticle. Epicuticlins are a family of tandem repeat cuticle proteins of unknown function. Here, we analyze the localization and function of the three C. elegans epicuticlins (EPIC proteins). EPIC-1 and EPIC-2 localize to the surface of the cuticle near the outer lipid layer, as well as to interfacial cuticles and adult-specific struts. EPIC-3 is expressed in dauer larvae and localizes to interfacial aECM in the buccal cavity. Skin wounding in the adult induces epic-3 expression, and EPIC proteins localize to wound sites. Null mutants lacking EPIC proteins are viable with reduced permeability barrier function and normal epicuticle lipid mobility. Loss of function in EPIC genes modifies the skin blistering phenotypes of Bli mutants and reduces survival after skin wounding. Our results suggest EPIC proteins define specific cortical compartments of the aECM and promote wound repair.
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