Depletion of vesicle-tethering factor p115 causes mini-stacked Golgi fragments with delayed protein transport

Biochem Biophys Res Commun. 2005 Dec 16;338(2):1268-74. doi: 10.1016/j.bbrc.2005.10.084. Epub 2005 Oct 24.

Abstract

Depletion of p115 with small interfering RNA caused fragmentation of the Golgi apparatus, resulting in dispersed distribution of stacked short cisternae and a vesicular structure (mini-stacked Golgi). The mini-stacked Golgi with cis- and trans-organization is functional in protein transport and glycosylation, although secretion is considerably retarded in p115 knockdown cells. The fragmented Golgi was further disrupted by treatment with breferdin A and reassembled into the mini-stacked Golgi by removal of the drug, as observed in control cells. In addition, p115 knockdown cells maintained retrograde transport from the Golgi to the endoplasmic reticulum, although the rate was not as efficient as in control cells. While no alternation of microtubule networks was found in p115 knockdown cells, the fragmented Golgi resembled those in cells treated with anti-microtubule drugs. The results suggest that p115 is involved in vesicular transport between endoplasmic reticulum and the Golgi, along with microtubule networks.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Drosophila Proteins / deficiency*
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure*
  • Gene Silencing
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure*
  • Golgi Matrix Proteins
  • HeLa Cells
  • Humans
  • Membrane Proteins / deficiency*
  • Protein Transport / physiology*

Substances

  • Drosophila Proteins
  • Golgi Matrix Proteins
  • Membrane Proteins
  • p115 protein, Drosophila