Rafts defined: a report on the Keystone symposium on lipid rafts and cell function

Linda J Pike

doi:10.1194/jlr.e600002-jlr200

Abstract

The recent Keystone Symposium on Lipid Rafts and Cell Function (March 23-28, 2006 in Steamboat Springs, CO) brought together biophysicists, biochemists, and cell biologists to discuss the structure and function of lipid rafts. What emerged from the meeting was a consensus definition of a membrane raft: "Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions." This definition helps to clarify current thinking in a field that has been plagued by the heterogeneous and sometimes ephemeral nature of its subject.

Highlights

The recent Keystone Symposium on Lipid Rafts and Cell Function (March 23–28, 2006 in Steamboat Springs, CO) brought together biophysicists, biochemists, and cell biologists to discuss the structure and function of lipid rafts
It is rare that a meeting is held to discuss an entity that is difficult to visualize, has an ill-defined molecular composition, and whose very existence has been questioned [1]. Such was the case in Steamboat Springs, CO, on March 23– 28, 2006, when the Keystone Symposium on Lipid Rafts and Cell Function was convened
Organized by Linda Pike (Washington University) and Michael Edidin ( Johns Hopkins University), the meeting brought together biophysicists, biochemists, and cell biologists to ponder the question, “What is a raft?”

Summary

Introduction

The recent Keystone Symposium on Lipid Rafts and Cell Function (March 23–28, 2006 in Steamboat Springs, CO) brought together biophysicists, biochemists, and cell biologists to discuss the structure and function of lipid rafts. The definition adopted by the group was as follows: “Membrane rafts are small (10–200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched domains that compartmentalize cellular processes.

Results

Conclusion