The function of GORASPs in Golgi apparatus organization in vivo

J Cell Biol. 2020 Sep 7;219(9):e202004191. doi: 10.1083/jcb.202004191.

Abstract

In vitro experiments have shown that GRASP65 (GORASP1) and GRASP55 (GORASP2) proteins function in stacking Golgi cisternae. However, in vivo depletion of GORASPs in metazoans has given equivocal results. We have generated a mouse lacking both GORASPs and find that Golgi cisternae remained stacked. However, the stacks are disconnected laterally from each other, and the cisternal cross-sectional diameters are significantly reduced compared with their normal counterparts. These data support earlier findings on the role of GORASPs in linking stacks, and we suggest that unlinking of stacks likely affects dynamic control of COPI budding and vesicle fusion at the rims. The net result is that cisternal cores remain stacked, but cisternal diameter is reduced by rim consumption.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COP-Coated Vesicles / metabolism
  • Female
  • Golgi Apparatus / metabolism*
  • Golgi Matrix Proteins / metabolism*
  • Intracellular Membranes / metabolism
  • Membrane Fusion / physiology
  • Membrane Proteins / metabolism
  • Mice
  • Mice, Inbred C57BL

Substances

  • Golgi Matrix Proteins
  • Gorasp1 protein, mouse
  • Gorasp2 protein, mouse
  • Membrane Proteins