{Reference Type}: Journal Article
{Title}: Dynamic movement of the Golgi unit and its glycosylation enzyme zones.
{Author}: Harada A;Kunii M;Kurokawa K;Sumi T;Kanda S;Zhang Y;Nadanaka S;Hirosawa KM;Tokunaga K;Tojima T;Taniguchi M;Moriwaki K;Yoshimura SI;Yamamoto-Hino M;Goto S;Katagiri T;Kume S;Hayashi-Nishino M;Nakano M;Miyoshi E;Suzuki KGN;Kitagawa H;Nakano A;
{Journal}: Nat Commun
{Volume}: 15
{Issue}: 1
{Year}: 2024 May 27
{Factor}: 17.694
{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.