The Golgi architecture and cell sensing

Biochem Soc Trans. 2018 Oct 19;46(5):1063-1072. doi: 10.1042/BST20180323. Epub 2018 Sep 20.

Abstract

An array of signalling molecules are located at the Golgi apparatus, including phosphoinositides, small GTPases, kinases, and phosphatases, which are linked to multiple signalling pathways. Initially considered to be associated predominantly with membrane trafficking, signalling pathways at the Golgi are now recognised to regulate a diverse range of higher-order functions. Many of these signalling pathways are influenced by the architecture of the Golgi. In vertebrate cells, the Golgi consists of individual stacks fused together into a compact ribbon structure and the function of this ribbon structure has been enigmatic. Notably, recent advances have identified a role for the Golgi ribbon in regulation of cellular processes. Fragmentation of the Golgi ribbon results in modulation of many signalling pathways. Various diseases and disorders, including cancer and neurodegeneration, are associated with the loss of the Golgi ribbon and the appearance of a dispersed fragmented Golgi. Here, we review the emerging theme of the Golgi as a cell sensor and highlight the relationship between the morphological status of the Golgi in vertebrate cells and the modulation of signalling networks.

Keywords: Golgi apparatus; Golgi ribbon; neurodegeneration; organelle structure; signalling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Cell Proliferation
  • Cytoskeleton / metabolism
  • DNA Damage
  • Glycosylation
  • Golgi Apparatus / metabolism*
  • Homeostasis
  • Humans
  • Lysosomes / metabolism
  • Mechanistic Target of Rapamycin Complex 1 / metabolism
  • Mitosis
  • Phosphatidylinositols / chemistry
  • Protein Transport*
  • Signal Transduction*
  • TOR Serine-Threonine Kinases / metabolism

Substances

  • Phosphatidylinositols
  • MTOR protein, human
  • Mechanistic Target of Rapamycin Complex 1
  • TOR Serine-Threonine Kinases