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Full-Length, Glycosylated Nsp4 Is Localized To Plasma Membrane Caveolae By A Novel Raft Isolation Technique, Stephen M. Storey, Thomas F. Gibbons, Cecelia V. Williams, Rebecca D. Parr, Friedhelm Schroeder, Judith M. Ball
Full-Length, Glycosylated Nsp4 Is Localized To Plasma Membrane Caveolae By A Novel Raft Isolation Technique, Stephen M. Storey, Thomas F. Gibbons, Cecelia V. Williams, Rebecca D. Parr, Friedhelm Schroeder, Judith M. Ball
Faculty Publications
Rotavirus NSP4, initially characterized as an endoplasmic reticulum intracellular receptor, is a multifunctional viral enterotoxin that induces diarrhea in murine pups. There have been recent reports of the secretion of a cleaved NSP4 fragment (residues 112 to 175) and of the association of NSP4 with LC3-positive autophagosomes, raft membranes, and microtubules. To determine if NSP4 traffics to a specific subset of rafts at the plasma membrane, we isolated caveolae from plasma membrane-enriched material that yielded caveola membranes free of endoplasmic reticulum and nonraft plasma membrane markers. Analyses of the newly isolated caveolae from rotavirus-infected MDCK cells revealed full-length, high-mannose glycosylated …
Sterol Carrier Protein-2 Directly Interacts With Caveolin-1 In Vitro And In Vivo, Minglong Zhou, Rebecca D. Parr, Anca D. Petrescu, H. Ross Payne, Barbara P. Atshaves, Ann B. Kier, Judith M. Ball, Friedhelm Schroeder
Sterol Carrier Protein-2 Directly Interacts With Caveolin-1 In Vitro And In Vivo, Minglong Zhou, Rebecca D. Parr, Anca D. Petrescu, H. Ross Payne, Barbara P. Atshaves, Ann B. Kier, Judith M. Ball, Friedhelm Schroeder
Faculty Publications
HDL-mediated reverse-cholesterol transport as well as phosphoinositide signaling are mediated through plasma membrane microdomains termed caveolae/lipid rafts. However, relatively little is known regarding mechanism(s) whereby these lipids traffic to or are targeted to caveolae/lipid rafts. Since sterol carrier protein-2 (SCP-2) binds both cholesterol and phosphatidylinositol, the possibility that SCP-2 might interact with caveolin-1 and caveolae was examined. Double immunolabeling and laser scanning fluorescence microscopy showed that a small but significant portion of SCP-2 colocalized with caveolin-1 primarily at the plasma membrane of L-cells and more so within intracellular punctuate structures in hepatoma cells. In SCP-2 overexpressing L-cells, SCP-2 was detected …