bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown
Published: Sept. 29, 2024
Abstract The outermost layer of cilia is a coat membrane anchored, glycosylated proteins often referred to as glycocalyx. This highly heterogeneous provides functions from regulation adhesion, force transduction and protection signalling. Despite its importance, there lack studies focusing on the high-resolution molecular architecture this layer. We describe structure ciliary green alga Chlamydomonas reinhardtii by cryo-electron tomography proteomic approaches present single particle analysis FMG1B via microscopy, most abundant constituent C. coat. report be unusual mucin orthologue which lacks major O -glycosylation mammalian mucins, but undergoes significant N -glycosylation. find that an isoform FMG1B, FMG1A, previously believed not expressed, in differentially regulated FMG1B. By micro-flow-based adhesion assays we observe increased surface glycocalyx deficient double-mutant fmg1a-fmg1b . mutant fully capable surface-gliding, suggesting neither required for extracellular intraflagellar transport. Our data provide in-depth structural details primary contact environment reveal FMG1 acts primarily protective with adhesion-regulative properties.
Language: Английский