Unwrapping the ciliary coat: high-resolution structure and function of the ciliary glycocalyx DOI
Lara Hoepfner, Adrian P. Nievergelt,

Fabrizio Matrino

et al.

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

Unwrapping the Ciliary Coat: High‐Resolution Structure and Function of the Ciliary Glycocalyx DOI Creative Commons
Lara Hoepfner, Adrian P. Nievergelt,

Fabrizio Matrino

et al.

Advanced Science, Journal Year: 2025, Volume and Issue: unknown

Published: March 5, 2025

The glycocalyx, a highly heterogeneous glycoprotein layer of cilia regulates adhesion and force transduction is involved in signaling. high-resolution molecular architecture this currently not understood. structure the ciliary coat described green alga Chlamydomonas reinhardtii by cryo-electron tomography proteomic approaches cryoEM main component, FMG1B solved. as mucin orthologue which lacks major O-glycosylation mammalian mucins but N-glycosylated. FMG1A, previously undescribed isoform expressed C. reinhardtii. By microflow-based assays, increased surface glycocalyx deficient double-mutant fmg1b-fmg1a observed. It found mutant capable surface-gliding, with neither required for extracellular intraflagellar transport. results find FMG1 to form protective adhesion-regulative instead adhesion-conferring properties an example class mucins.

Language: Английский

Citations

0
Unwrapping the ciliary coat: high-resolution structure and function of the ciliary glycocalyx DOI
Lara Hoepfner, Adrian P. Nievergelt,

Fabrizio Matrino

et al.

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

Citations

1