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A collagen IV fluorophore knock-in toolkit reveals trimer diversity in <i>C. elegans</i> basement membranes

Sandhya Srinivasan, William Ramos-Lewis, Mychel Morais, Qiuyi Chi, Adam W. J. Soh, E. G. Williams, Rachel Lennon, David R. Sherwood

2025The Journal of Cell Biology12 citationsDOIOpen Access PDF

Abstract

The type IV collagen triple helix, composed of three ⍺-chains, is a core basement membrane (BM) component that assembles into a network within BMs. Endogenous tagging of all ⍺-chains with genetically encoded fluorophores has remained elusive, limiting our understanding of this crucial BM component. Through genome editing, we show that the C termini of the C. elegans type IV collagen ⍺-chains EMB-9 and LET-2 can be fused to a variety of fluorophores to create a strain toolkit with wild-type health. Using quantitative imaging, our results suggest a preference for LET-2-LET-2-EMB-9 trimer construction, but also tissue-specific flexibility in trimers assembled driven by differences in ⍺-chain expression levels. By tagging emb-9 and let-2 mutants that model human Gould syndrome, a complex multitissue disorder, we further discover defects in extracellular accumulation and turnover that might help explain disease pathology. Together, our findings identify a permissive tagging site in C. elegans that will allow diverse studies on type IV collagen regulation and function in animals.

Topics & Concepts

TrimerTriple helixMutantExtracellular matrixBasement membraneFluorophoreMembraneCaenorhabditis elegansChemistryBiologyCell biologyBiophysicsComputational biologyBiochemistryGeneStereochemistryFluorescencePhysicsOrganic chemistryDimerQuantum mechanicsGenetics, Aging, and Longevity in Model OrganismsCellular Mechanics and Interactions3D Printing in Biomedical Research