Publication Date:
2002-06-08
Description:
The surface membrane of cells is studded with morphologically distinct regions, or domains, like microvilli, cell-cell junctions, and coated pits. Each of these domains is specialized for a particular function, such as nutrient absorption, cell-cell communication, and endocytosis. Lipid domains, which include caveolae and rafts, are one of the least understood membrane domains. These domains are high in cholesterol and sphingolipids, have a light buoyant density, and function in both endocytosis and cell signaling. A major mystery, however, is how resident molecules are targeted to lipid domains. Here, we propose that the molecular address for proteins targeted to lipid domains is a lipid shell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, Richard G W -- Jacobson, Ken -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA. richard.anderson@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052946" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Caveolae/chemistry/*metabolism/ultrastructure
;
Cholesterol/chemistry/*metabolism
;
Glycosylphosphatidylinositols/chemistry/metabolism
;
Humans
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Lipid Bilayers
;
Membrane Microdomains/chemistry/*metabolism/ultrastructure
;
Membrane Proteins/chemistry/*metabolism
;
Protein Binding
;
*Protein Transport
;
Sphingolipids/chemistry/*metabolism
;
Static Electricity
;
Thermodynamics
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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