The ER/Golgi Interface - Is There Anything in-between?

Chris Hawes

doi:10.3389/fpls.2012.00073

Abstract

OPINION article Front. Plant Sci., 18 April 2012Sec. Plant Cell Biology Volume 3 - 2012 | https://doi.org/10.3389/fpls.2012.00073

Highlights

Endoplasmic reticulum export sites (ERES) are specific domains on the ER surface where cargo proteins, both soluble and membrane-bound, exit the ER in transit to the cis-side of the Golgi apparatus for processing and secretion
Conventional transmission electron microscopy (TEM) of higher plants has not revealed the presence of visible coated areas on ER membranes or any structures that could be convincingly interpreted as ERES
Immunolabeling of COPII components has suggested that exit site proteins could exist on the ER separate from Golgi bodies (Yang et al, 2005; Zhang et al, 2010), almost all data from live cell imaging suggests a close association between the two structures (Hanton et al, 2009; Langhans et al, 2012)

Summary

Introduction

Endoplasmic reticulum export sites (ERES) are specific domains on the ER surface where cargo proteins, both soluble and membrane-bound, exit the ER in transit to the cis-side of the Golgi apparatus for processing and secretion. At the same time a live cell imaging approach based around the expression of fluorescent protein markers indicated that Golgi bodies are intimately associated with the ER, and that the two organelles may even be connected together (Boevink et al, 1998; daSilva et al, 2004; Faso et al, 2009).

Results

Conclusion