Organelles pp 60-79 | Cite as

The Endoplasmic Reticulum

  • Mark Carroll
Part of the Macmillan Molecular Biology Series book series


The endoplasmic reticulum (ER) may form up to half of the cell’s total membrane (table 1.1). This proportion is strikingly high in those cells specialised for the export of lipids (such as hepatocytes and cells of the gonads) or of proteins (such as pancreatic cells or certain classes of B lymphocytes). However, almost all cells contain an extensive array of membranes that can be seen under the electron microscope to ramify throughout the cytosol (as in figure 1.3). Biochemical characterisation of he ER has been aided by the tendency of its membranes to fragment into small vesicles during during homogenisation of tissue samples. The resulting ‘microsomes’ can be readily prepared by centrifugation (section 2.2.1). As we shall see, microsomes have been widely used as cell-free model systems for studying many of the biosynthetic processes mediated by the ER.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

4.7 Further reading

Lipid biosynthesis

  1. Coleman, R. and Bell, R. M. (1978). J. Cell Biol., 76, 245–253. (Asymmetric phospholipid synthesis by the smooth ER)CrossRefGoogle Scholar
  2. Bloch, K. (1965). Science, 150, 19–28. (Cholesterol synthesis)CrossRefGoogle Scholar

Translocation of membrane proteins

  1. Blobel, G. and Dobberstein, B. (1975). J. Cell Biol., 67, 835–253. (The signal peptide hypothesis)CrossRefGoogle Scholar
  2. Evans, E. A., Gilmore, R. and Blobel, G. (1986). Proc. Nat. Acad. Sci. USA, 83, 581–585. (The signal peptidase complex)CrossRefGoogle Scholar
  3. Walter, P., Gilmore, R. and Blobel, G. (1984). Cell, 38, 5–8. (Protein translocation across the ER)CrossRefGoogle Scholar

Post-translational processing

  1. Eyre, D. R. (1980). Science, 207, 1315–1322. (Biosynthesis of collagen)CrossRefGoogle Scholar
  2. Kornfeld, R. and Kornfeld, S. (1985). Ann. Rev. Biochem., 54, 631–664. (N-linked glycosylation of proteins)CrossRefGoogle Scholar
  3. Sefton, B. M. and Buss, J. E. (1987). J. Cell Biol., 104, 1449–1453. (Fatty acylation of proteins)CrossRefGoogle Scholar

Membrane function (selected aspects)

  1. Rothman, J. E. and Lenard, J. (1977). Science, 195, 743–753. (The significance of membrane asymmetry)CrossRefGoogle Scholar
  2. Berridge, M. J. (1987). Ann. Rev. Biochem., 56, 159–193. (Phosphoinositides and stimulus-response coupling)CrossRefGoogle Scholar
  3. Nebert, D. W. and Gonzalez, F. J. (1987). Ann. Rev. Biochem., 56, 945–993. (The cytochrome P450 super-family)CrossRefGoogle Scholar

Copyright information

© Mark Carroll 1989

Authors and Affiliations

  • Mark Carroll
    • 1
  1. 1.Department of BiochemistryThe London Hospital Medical CollegeLondonUK

Personalised recommendations