{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T05:06:56Z","timestamp":1791176816061,"version":"4.1.0"},"reference-count":0,"publisher":"Rockefeller University Press","issue":"4","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1993,8,15]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1083\/jcb.122.4.789","type":"journal-article","created":{"date-parts":[[2004,5,15]],"date-time":"2004-05-15T00:22:22Z","timestamp":1084580542000},"page":"789-807","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":758,"title":["Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells"],"prefix":"10.1083","volume":"122","author":[{"given":"M","family":"Sargiacomo","sequence":"first","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Sudol","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Z","family":"Tang","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"MP","family":"Lisanti","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1993,8,15]]},"container-title":["The Journal of cell biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/122\/4\/789\/1474701\/789.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/122\/4\/789\/1474701\/789.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T04:30:38Z","timestamp":1690000238000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/122\/4\/789\/14742\/Signal-transducing-molecules-and-glycosyl"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,8,15]]},"references-count":0,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1993,8,15]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.122.4.789","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,8,15]]}}}