Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Journal Club
  • Published:

Choosing who can ride the raft

Nature Reviews Molecular Cell Biology volume 21, pages 566–567 (2020)Cite this article

Subjects

The idea that cellular membranes are laterally heterogeneous, harbouring distinct, ordered microdomains — lipid (or membrane) rafts — has become a key concept in cell biology, although it is still considered a hypothesis. The origins of the raft model can be traced back to an elegant 1992 Cell paper by Brown and Rose, which reported that GPI-anchored proteins associate with detergent-resistant, membranous complexes enriched in glycosphingolipids when trafficking from the Golgi complex to the apical surface of polarized epithelial cells. These findings implied the existence of protein and sphingolipid-enriched microdomains that are capable of sorting membrane proteins and directing their intracellular transport, and defined a convenient biochemical assay to study them. They went on to demonstrate that these membranes contained a 1:1:1 mixture of cholesterol, glycerophospholipids and sphingolipids. This membrane composition was shortly thereafter linked to the liquid-ordered phase of membranes, now thought to represent the characteristic state of raft lipids. Finally, they speculated that microdomains may be more generally involved in protein sorting and trafficking, even in non-polarized cells.

Ideas that ultimately evolved from Brown and Rose’s findings — the notion that the lipid composition of the plasma membrane can support the formation of co-existing liquid-ordered and liquid-disordered phases and that GPI anchors endow proteins with high affinity for ordered membrane domains — have become firmly entrenched in the literature. Yet, today, most would agree that detergent-resistant membranes studied by Brown and Rose cannot be directly equated to rafts, and many important questions about rafts remain elusive.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

References

Original articles

  • Brown, D. A. & Rose, J. K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533–544 (1992)

    Article  CAS  Google Scholar 

  • Lorent, J. H. et al. Structural determinants and functional consequences of protein affinity for membrane rafts. Nat. Commun. 8, 1219 (2017)

    Article  Google Scholar 

Related article

  • Sezgin, E. et al. The mystery of membrane organization: composition, regulation and roles of lipid rafts. Nat. Rev. Mol. Cell Biol. 18, 361–374 (2017)

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Center for Membrane and Cell Physiology, University of Virginia School of Medicine, Charlottesville, VA, USA

    Anne K. Kenworthy

Authors
  1. Anne K. Kenworthy
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Anne K. Kenworthy.

Ethics declarations

Competing interests

The author declares no competing interests.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Kenworthy, A.K. Choosing who can ride the raft. Nat Rev Mol Cell Biol 21, 566–567 (2020). https://doi.org/10.1038/s41580-020-00285-y

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41580-020-00285-y

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing