FEBS Letters
Volume 580, Issue 9 , Pages 2160-2165, 17 April 2006

Endoplasmic reticulum: A metabolic compartment

Edited by Felix Wieland

  • Miklós Csala

      Affiliations

    • Deptartment of Medical Chemistry, Semmelweis University and Endoplasmic Reticulum Research Group of the Hungarian Academy of Sciences, 1444 Budapest, Hungary
  • ,
  • Gábor Bánhegyi

      Affiliations

    • Department of Physiopathology, Experimental Medicine and Public Health, University of Siena, Viale Aldo Moro, 43100 Siena, Italy
  • ,
  • Angelo Benedetti

      Affiliations

    • Department of Physiopathology, Experimental Medicine and Public Health, University of Siena, Viale Aldo Moro, 43100 Siena, Italy
    • Unit for Development of Biomedical Research, Santa Maria alle Scotte Hospital, 53100 Siena, Italy
    • Corresponding Author InformationCorresponding author. Fax: +39 0577 234 009.

Received 3 February 2006; received in revised form 7 March 2006; accepted 15 March 2006. published online 27 March 2006.

Abstract 

Several biochemical reactions and processes of cell biology are compartmentalized in the endoplasmic reticulum (ER). The view that the ER membrane is basically a scaffold for ER proteins, which is permeable to small molecules, is inconsistent with recent findings. The luminal micro-environment is characteristically different from the cytosol; its protein and glutathione thiols are remarkably more oxidized, and it contains a separate pyridine nucleotide pool. The substrate specificity and activity of certain luminal enzymes are dependent on selective transport of possible substrates and co-factors from the cytosol. Abundant biochemical, pharmacological, clinical and genetic data indicate that the barrier function of the lipid bilayer and specific transport activities in the membrane make the ER a separate metabolic compartment.

Abbreviations: ER, endoplasmic reticulum, GSH, glutathione, GSSG, glutathione disulfide, GSD 1, glycogen storage disease type 1, CRD, cortisone reductase deficiency, G6P, glucose-6-phosphate, G6Pase, glucose-6-phosphatase, G6PT, glucose-6-phosphate transporter, H6PDH, hexose-6-phosphate dehydrogenase, 11βHSDH1, 11β-hydroxysteroid dehydrogenase type 1, MHC, major histocompatibility complex, RER, rough endoplasmic reticulum, TAP, transporter associated with antigen processing, UGA, UDP-glucuronic acid, UGT, UDP-glucuronosyltransferase

Keywords: Endoplasmic reticulum, Membrane, Permeability, Transport, Compartment, Barrier, Latency, Specificity, Lumen

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(06)00365-6

doi:10.1016/j.febslet.2006.03.050

FEBS Letters
Volume 580, Issue 9 , Pages 2160-2165, 17 April 2006