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• W2064754325 endingPage "807" @default.
• W2064754325 startingPage "789" @default.
• W2064754325 abstract "GPI-linked protein molecules become Triton-insoluble during polarized sorting to the apical cell surface of epithelial cells. These insoluble complexes, enriched in cholesterol, glycolipids, and GPI-linked proteins, have been isolated by flotation on sucrose density gradients and are thought to contain the putative GPI-sorting machinery. As the cellular origin and molecular protein components of this complex remain unknown, we have begun to characterize these low-density insoluble complexes isolated from MDCK cells. We find that these complexes, which represent 0.4-0.8% of the plasma membrane, ultrastructurally resemble caveolae and are over 150-fold enriched in a model GPI-anchored protein and caveolin, a caveolar marker protein. However, they exclude many other plasma membrane associated molecules and organelle-specific marker enzymes, suggesting that they represent microdomains of the plasma membrane. In addition to caveolin, these insoluble complexes contain a subset of hydrophobic plasma membrane proteins and cytoplasmically-oriented signaling molecules, including: (a) GTP-binding proteins--both small and heterotrimeric; (b) annex II--an apical calcium-regulated phospholipid binding protein with a demonstrated role in exocytic fusion events; (c) c-Yes--an apically localized member of the Src family of non-receptor type protein-tyrosine kinases; and (d) an unidentified serine-kinase activity. As we demonstrate that caveolin is both a transmembrane molecule and a major phospho-acceptor component of these complexes, we propose that caveolin could function as a transmembrane adaptor molecule that couples luminal GPI-linked proteins with cytoplasmically oriented signaling molecules during GPI-membrane trafficking or GPI-mediated signal transduction events. In addition, our results have implications for understanding v-Src transformation and the actions of cholera and pertussis toxins on hetero-trimeric G proteins." @default.
• W2064754325 created "2016-06-24" @default.
• W2064754325 creator A5016681558 @default.
• W2064754325 creator A5031243945 @default.
• W2064754325 creator A5058298248 @default.
• W2064754325 creator A5063607950 @default.
• W2064754325 date "1993-08-15" @default.
• W2064754325 modified "2023-10-10" @default.
• W2064754325 title "Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells" @default.
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• W2064754325 doi "https://doi.org/10.1083/jcb.122.4.789" @default.
• W2064754325 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2119592" @default.
• W2064754325 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8349730" @default.
• W2064754325 hasPublicationYear "1993" @default.
• W2064754325 type Work @default.
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