Cholesterol is critical to the integrity of neuronal porosome/fusion pore
Write to authors to ask them to make this article freely available at NoL Archive
Ultramicroscopy. 2006 Jun-Jul;106(8-9):674-7. Epub 2006 Apr 19
Jeremic A, Jin Cho W, Jena BP.
Department of Physiology, Wayne State University School of Medicine, Detroit, MI, 48201, USA.
Secretion is one of the most fundamental cellular processes. Porosomes have been demonstrated as the universal secretory machinery in cells. Earlier studies determine the presence of a number of proteins in porosomes, among them the N- and P/Q-type calcium channels, actin, syntaxin-1, synaptotagmin-1, vimentin, the N-ethylmaleimide-sensitive factor (NSF), the chloride channel CLC-3, and the alpha subunit of the heterotrimeric GTP-binding protein G(o). Studies demonstrate that t-SNAREs localize at the base of porosomes, and directly interact with calcium channels. In the present study, we demonstrate that Syntaxin-1 co-localizes with cholesterol in solubilized synaptosomal membrane preparations. Depletion of cholesterol, results in the dissociation of both Syntaxin-1 and N-type calcium channel from neuronal porosomes. Thus, cholesterol participates as an integral component of the neuronal porosome complex, and is required for its stability.
PubMed ID and Record
Ultramicroscopy. 2006 Jun-Jul;106(8-9):674-7. Epub 2006 Apr 19
Jeremic A, Jin Cho W, Jena BP.
Department of Physiology, Wayne State University School of Medicine, Detroit, MI, 48201, USA.
Secretion is one of the most fundamental cellular processes. Porosomes have been demonstrated as the universal secretory machinery in cells. Earlier studies determine the presence of a number of proteins in porosomes, among them the N- and P/Q-type calcium channels, actin, syntaxin-1, synaptotagmin-1, vimentin, the N-ethylmaleimide-sensitive factor (NSF), the chloride channel CLC-3, and the alpha subunit of the heterotrimeric GTP-binding protein G(o). Studies demonstrate that t-SNAREs localize at the base of porosomes, and directly interact with calcium channels. In the present study, we demonstrate that Syntaxin-1 co-localizes with cholesterol in solubilized synaptosomal membrane preparations. Depletion of cholesterol, results in the dissociation of both Syntaxin-1 and N-type calcium channel from neuronal porosomes. Thus, cholesterol participates as an integral component of the neuronal porosome complex, and is required for its stability.
PubMed ID and Record
0 Comments:
Post a Comment
<< Home