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Structure and function of membrane rafts.

Deborah Brown1

  • 1Department of Biochemistry and Cell Biology, SUNY at Stony Brook, NY 11794-5215, USA. deborah.brown@sunysb.edu

International Journal of Medical Microbiology : IJMM
|March 14, 2002
PubMed
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Cell membranes contain specialized lipid rafts, enriched in cholesterol and sphingolipids. These microdomains influence protein function and signal transduction in various cellular processes.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Biophysics

Background:

  • Cell membranes are complex lipid bilayers where lipids can form distinct microdomains.
  • Cholesterol and sphingolipid-rich microdomains, known as rafts, are proposed to exist in a liquid-ordered phase.

Purpose of the Study:

  • To review membrane lipid phase behavior and differentiate between liquid-crystalline, liquid-ordered, and gel phases.
  • To present evidence for the coexistence of phospholipid-rich and sphingolipid-rich domains in biological membranes.
  • To explore the role of rafts in membrane protein targeting and function.

Main Methods:

  • Review of membrane lipid phase behavior.
  • Analysis of evidence for coexisting lipid domains in biological membranes.

Related Experiment Videos

  • Examination of protein partitioning into specific membrane microdomains.
  • Main Results:

    • Evidence suggests phospholipid-rich liquid-crystalline and sphingolipid-rich liquid-ordered domains (rafts) coexist in equilibrium, particularly in plasma membranes.
    • Membrane proteins, including glycosyl phosphatidylinositol (GPI)-anchored proteins and those with saturated acyl chains, preferentially partition into rafts.
    • This preferential targeting impacts protein function.

    Conclusions:

    • Lipid rafts are functional microdomains within cell membranes.
    • Rafts play significant roles in signal transduction, intracellular sorting, and regulation of cell-surface proteolysis.
    • Understanding raft dynamics is crucial for comprehending diverse cellular functions.