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      Lipid Rafts, Detergent-Resistant Membranes, and Raft Targeting Signals

      Author(s): 1
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      Journal: Physiology
      Publisher: American Physiological Society

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          Abstract

          Lipid rafts are liquid-ordered (l o) phase microdomains proposed to exist in biological membranes. Rafts have been widely studied by isolating l o-phase detergent-resistant membranes (DRMs) from cells. Recent findings have shown that DRMs are not the same as preexisting rafts, prompting a major revision of the raft model. Nevertheless, raft-targeting signals identified by DRM analysis are often required for protein function, implicating rafts in a variety of cell processes.

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          Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells.

          David Zacharias, Jonathan D Violin, Alexandra C Newton … (2002)
          Many proteins associated with the plasma membrane are known to partition into submicroscopic sphingolipid- and cholesterol-rich domains called lipid rafts, but the determinants dictating this segregation of proteins in the membrane are poorly understood. We suppressed the tendency of Aequorea fluorescent proteins to dimerize and targeted these variants to the plasma membrane using several different types of lipid anchors. Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts. Thus the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.
          Article 0 comments Cited 529 times – based on 0 reviews     Review now
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            Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly.

            Jamil S. Saad, Jaime Miller, Janet Tai … (2006)
            During the late phase of HIV type 1 (HIV-1) replication, newly synthesized retroviral Gag proteins are targeted to the plasma membrane of most hematopoietic cell types, where they colocalize at lipid rafts and assemble into immature virions. Membrane binding is mediated by the matrix (MA) domain of Gag, a 132-residue polypeptide containing an N-terminal myristyl group that can adopt sequestered and exposed conformations. Although exposure is known to promote membrane binding, the mechanism by which Gag is targeted to specific membranes has yet to be established. Recent studies have shown that phosphatidylinositol (PI) 4,5-bisphosphate [PI(4,5)P(2)], a factor that regulates localization of cellular proteins to the plasma membrane, also regulates Gag localization and assembly. Here we show that PI(4,5)P(2) binds directly to HIV-1 MA, inducing a conformational change that triggers myristate exposure. Related phosphatidylinositides PI, PI(3)P, PI(4)P, PI(5)P, and PI(3,5)P(2) do not bind MA with significant affinity or trigger myristate exposure. Structural studies reveal that PI(4,5)P(2) adopts an "extended lipid" conformation, in which the inositol head group and 2'-fatty acid chain bind to a hydrophobic cleft, and the 1'-fatty acid and exposed myristyl group bracket a conserved basic surface patch previously implicated in membrane binding. Our findings indicate that PI(4,5)P(2) acts as both a trigger of the myristyl switch and a membrane anchor and suggest a potential mechanism for targeting Gag to membrane rafts.
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              Lipid rafts: contentious only from simplistic standpoints.

              F Hancock (2006)
              The hypothesis that lipid rafts exist in plasma membranes and have crucial biological functions remains controversial. The lateral heterogeneity of proteins in the plasma membrane is undisputed, but the contribution of cholesterol-dependent lipid assemblies to this complex, non-random organization promotes vigorous debate. In the light of recent studies with model membranes, computational modelling and innovative cell biology, I propose an updated model of lipid rafts that readily accommodates diverse views on plasma-membrane micro-organization.
              Article 0 comments Cited 137 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Title: Physiology
                Abbreviated Title: Physiology
                Publisher: American Physiological Society
                ISSN (Print): 1548-9213
                ISSN (Electronic): 1548-9221
                Publication date Created: December 2006
                Publication date (Print): December 2006
                Volume: 21
                Issue: 6
                Pages: 430-439
                Affiliations
                [1 ]Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York,
                Article
                DOI: 10.1152/physiol.00032.2006
                PubMed ID: 17119156
                SO-VID: 39e91856-a1f1-4dfa-bf38-8dc69bb3d67f
                Copyright © © 2006
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