Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane

被引:271
作者
Lajoie, Patrick [1 ]
Goetz, Jacky G. [1 ]
Dennis, James W. [2 ]
Nabi, Ivan R. [1 ]
机构
[1] Univ British Columbia, Inst Life Sci, Dept Cellular & Physiol Sci, Vancouver, BC V6T 1Z3, Canada
[2] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Toronto, ON M5G 1X5, Canada
基金
加拿大健康研究院;
关键词
SINGLE-MOLECULE TRACKING; FOCAL ADHESION DYNAMICS; PHOSPHORYLATED CAVEOLIN-1; ANCHORED PROTEINS; N-GLYCOSYLATION; CELL-RECEPTOR; LIPID RAFTS; ENDOCYTOSIS; CHOLESTEROL; ACTIVATION;
D O I
10.1083/jcb.200811059
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The plasma membrane is organized into various sub-domains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell-cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such as lipid rafts and lectin-glycoprotein lattices. Domains are organized by specialized scaffold proteins including the intramembranous caveolins, which stabilize lipid raft domains, and the galectins, a family of animal lectins that cross-link glycoproteins forming molecular lattices. We review evidence that these heterogeneous microdomains interact to regulate substratum adhesion and cytokine receptor dynamics at the cell surface.
引用
收藏
页码:381 / 385
页数:5
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