Cholesterol depletion blocks redistribution of lipid raft components and insulin-mimetic signaling by glimepiride and phosphoinositolglycans in rat adipocytes.
作者： Günter Müller , Nils Hanekop , Susanne Wied , Wendelin Frick
DOI: 10.1007/BF03402005
关键词: Dig 、 Caveolin 、 Cell biology 、 Cell membrane 、 Biology 、 Tyrosine kinase 、 Raft 、 Lipid raft 、 Membrane protein 、 Biochemistry 、 Signal transduction
摘要: Glycosylphosphatidylinositol-anchored plasma membrane (GPI) proteins, such as Gce1, the dually acylated nonreceptor tyrosine kinases (NRTKs), pp59Lyn, and protein, caveolin, together with cholesterol are typical components of detergent/carbonate-insoluble glycolipid-enriched raft domains (DIGs) in most eucaryotes. Previous studies demonstrated dissociation from caveolin concomitant redistribution DIGs Gce1 pp59Lyn rat adipocytes response to four different insulin-mimetic stimuli, glimepiride, phosphoinositolglycans, caveolin-binding domain peptide, trypsin/NaCl-treatment. We now characterized structural basis for this dynamic DIG components.
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