Dynamic movement of the Golgi unit and its glycosylation enzyme zones

Nat Commun. 2024 May 27;15(1):4514. doi: 10.1038/s41467-024-48901-1.

Abstract

Knowledge on the distribution and dynamics of glycosylation enzymes in the Golgi is essential for better understanding this modification. Here, using a combination of CRISPR/Cas9 knockin technology and super-resolution microscopy, we show that the Golgi complex is assembled by a number of small 'Golgi units' that have 1-3 μm in diameter. Each Golgi unit contains small domains of glycosylation enzymes which we call 'zones'. The zones of N- and O-glycosylation enzymes are colocalised. However, they are less colocalised with the zones of a glycosaminoglycan synthesizing enzyme. Golgi units change shapes dynamically and the zones of glycosylation enzymes rapidly move near the rim of the unit. Photobleaching analysis indicates that a glycosaminoglycan synthesizing enzyme moves between units. Depletion of giantin dissociates units and prevents the movement of glycosaminoglycan synthesizing enzymes, which leads to insufficient glycosaminoglycan synthesis. Thus, we show the structure-function relationship of the Golgi and its implications in human pathogenesis.

MeSH terms

  • CRISPR-Cas Systems
  • Glycosaminoglycans* / metabolism
  • Glycosylation
  • Golgi Apparatus* / metabolism
  • Golgi Matrix Proteins
  • HeLa Cells
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism

Substances

  • Glycosaminoglycans
  • macrogolgin
  • Membrane Proteins
  • Golgi Matrix Proteins