ER structure and function

Curr Opin Cell Biol. 2013 Aug;25(4):428-33. doi: 10.1016/ Epub 2013 Mar 13.


The ER forms a contiguous structure of interconnected sheets and tubules that spreads from the nuclear envelope to the cell cortex. Through its attachment to the cytoskeleton, the ER undergoes dynamic rearrangements, such as tubule extension and movement. ER shaping proteins (reticulons and DP1/Yop1p) play key roles in generating and maintaining the unique reticular morphology of the ER. Atlastin and its yeast homologue, Sey1p, mediate homotypic ER membrane fusion, which leads to the formation of new three-way junctions within the polygonal network. At these junctions, the Lunapark protein, Lnp1p, works in conjunction with the reticulons, DP1/Yop1p, and in antagonism to atlastin/Sey1p to maintain the network in a dynamic equilibrium. Defects in ER morphology have been linked to certain neurological disorders.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cytoskeleton / metabolism
  • Endoplasmic Reticulum / chemistry*
  • Endoplasmic Reticulum / metabolism*
  • Humans
  • Membrane Fusion
  • Membrane Proteins / metabolism
  • Microtubules / metabolism
  • Nuclear Envelope / metabolism
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism


  • Membrane Proteins