Molecular basis for sculpting the endoplasmic reticulum membrane

Int J Biochem Cell Biol. 2012 Sep;44(9):1436-43. doi: 10.1016/j.biocel.2012.05.013. Epub 2012 May 26.


The endoplasmic reticulum (ER) is involved in many critical processes, including protein and lipid synthesis and calcium storage. Morphologically, the ER can be divided into two subdomains: a network of interconnected tubules and interspersed sheets. Until recently, how these different compartments form in a continuous membrane system was unclear. Several classes of integral membrane proteins have been identified in the ER; the reticulons and DP1/Yop1p play roles in the generation of ER tubules, and possibly in stabilizing ER sheets, atlastins and Sey1p are dynamin-like GTPases that facilitate tubular network formation by mediating ER membrane fusion, and Climp63, p180, and kinectin are enriched in ER sheets and influence their formation. In this review, we summarize recent advances in our understanding of how these proteins participate in ER shaping. We also discuss possible mechanisms for regulating ER morphology via the cytoskeleton. Lessons learned about sculpting the ER membrane may be applicable to other organelles.

Publication types

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

MeSH terms

  • Animals
  • Endoplasmic Reticulum / metabolism*
  • Humans
  • In Vitro Techniques
  • Intracellular Membranes / chemistry
  • Intracellular Membranes / metabolism*
  • Membrane Proteins / metabolism
  • Microtubules / chemistry
  • Microtubules / metabolism
  • Nuclear Envelope / metabolism


  • Membrane Proteins