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Carbonic Anhydrase 3 Overexpression Modulates Signal-ling Pathways Associated with Cellular Stress Resilience and Proteostasis

ABSTRACT: The impact of CA3 overexpression on cellular pathways was investigated in HEK293T, MDA-MB-231, and SVCT cells using RNA sequencing and proteomics.

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ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell

DISEASE(S): Breast Cancer

SUBMITTER: Merrina Anugraham

LAB HEAD: Daniel Kolarich

PROVIDER: PXD071664 | Pride | 2025-12-15

REPOSITORIES: Pride

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Project description:The outermost layer of eukaryotic cilia is a coat of membrane anchored, glycosylated proteins often referred to as glycocalyx. This highly heterogeneous layer provides functions from regulation of adhesion, force transduction and protection to signaling. We describe the structure of the ciliary coat of the green alga Chlamydomonas by cryo-electron tomography and proteomic approaches and present the high-resolution single particle structure of FMG1B via cryo-electron microscopy, the most abundant constituent of the ciliary coat. We report FMG1B to be a highly unusual mucin orthologue, which lacks the major O-glycosylation of mammalian mucins, but undergoes significant N-glycosylation. We find that an isoform of FMG1-B, FMG1-A, previously believed to be not expressed, is present in Chlamydomonas and differentially regulated with FMG1-B. By micro-flow-based adhesion assays, we observe increased surface adhesion in the glycocalyx deficient double-mutant fmg1a-fmg1b. We find this mutant to be fully capable of surface-gliding, suggesting that neither isoform is required for extracellular force transduction by intraflagellar transport. Our data provide in-depth structural details of the ciliary coat that functions as the primary contact to the environment and reveal that FMG1 acts primarily as a protective layer with adhesion-regulative properties. Data deposited here include label free quantification data on whole cells or isolated cilia confirming single knockout of FMG1B and high abundance of FMG1A in CC4533fmg1b (combined_protein_WC_CC4533fmg1b.tsv ) and double knockout of FMG1A and FMG1B in M32fmg1afmg1b (combined_proteinCilia_M32_M32fmg1afmg1b.tsv). The latter dataset was further analyzed for abundance changes in the cilia proteome (Log2_LFQ_ratios_M32_M32fmg1afmg1b.csv). Further, isolated cilia of wild type M32 were analyzed under non-reducing conditions to confirm structure predicted disulfide bridges via LC-MS/MS in FMG1B (FMG1B_intraprotein_disulfides.xlsx). Finally, isolated cilia of M32 were subjected to N-glycopeptide analyses using InSource-CID (FMG1B_HexNAc_modified_peptides.xlsx).

			Action	DRS
	YY__1_2_250711.mzML	Mzml
	YY__1_2_250711.mzid	Mzid
	YY__1_5_250711.mzML	Mzml
	YY__1_5_250711.mzid	Mzid
	YY__2_1_250711.mzML	Mzml

Dataset Information

Carbonic Anhydrase 3 Overexpression Modulates Signal-ling Pathways Associated with Cellular Stress Resilience and Proteostasis

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