O-glycan initiation directs distinct biological pathways and controls epithelial differentiation

EMBO Rep. 2020 Jun 4;21(6):e48885. doi: 10.15252/embr.201948885. Epub 2020 Apr 23.

Abstract

Post-translational modifications (PTMs) greatly expand the function and potential for regulation of protein activity, and O-glycosylation is among the most abundant and diverse PTMs. Initiation of O-GalNAc glycosylation is regulated by 20 distinct GalNAc-transferases (GalNAc-Ts), and deficiencies in individual GalNAc-Ts are associated with human disease, causing subtle but distinct phenotypes in model organisms. Here, we generate a set of isogenic keratinocyte cell lines lacking either of the three dominant and differentially expressed GalNAc-Ts. Through the ability of keratinocytes to form epithelia, we investigate the phenotypic consequences of the loss of individual GalNAc-Ts. Moreover, we probe the cellular responses through global transcriptomic, differential glycoproteomic, and differential phosphoproteomic analyses. We demonstrate that loss of individual GalNAc-T isoforms causes distinct epithelial phenotypes through their effect on specific biological pathways; GalNAc-T1 targets are associated with components of the endomembrane system, GalNAc-T2 targets with cell-ECM adhesion, and GalNAc-T3 targets with epithelial differentiation. Thus, GalNAc-T isoforms serve specific roles during human epithelial tissue formation.

Keywords: 3D skin; differential glycoproteomics; polyomics; polypeptide GalNAc-transferase; tissue development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Differentiation
  • Epithelium / metabolism
  • Glycosylation
  • Humans
  • N-Acetylgalactosaminyltransferases* / genetics
  • N-Acetylgalactosaminyltransferases* / metabolism
  • Polysaccharides
  • Protein Processing, Post-Translational

Substances

  • Polysaccharides
  • N-Acetylgalactosaminyltransferases

Associated data

  • GEO/GSE141387