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J. Biol. Chem., Vol. 279, Issue 46, 47610-47618, November 12, 2004

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Ganglioside GD3 Traffics from the trans-Golgi Network to Plasma Membrane by a Rab11-independent and Brefeldin A-insensitive Exocytic Pathway^*

Pilar Maria Crespo, Ramiro Iglesias-Bartolomé¶, and Jose Luis Daniotti||

From the Centro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC (UNC-CONICET), Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, 5000 Córdoba, Argentina

Gangliosides, complex glycosphingolipids containing sialic acids, have been found to reside in glycosphingolipid-enriched microdomains (GEM) at the plasma membrane. They are synthesized in the lumen of the Golgi complex and appear unable to translocate from the lumenal toward the cytosolic surface of Golgi membrane to access the monomeric lipid transport. As a consequence, they can only leave the Golgi complex via the lumenal surface of transport vesicles. In this work we analyzed the exocytic transport of the disialo ganglioside GD3 from trans-Golgi network (TGN) to plasma membrane in CHO-K1 cells by immunodetection of endogenously synthesized GD3. We found that ganglioside GD3, unlike another luminal membrane-bounded lipid (glycosylphosphatidylinositol-anchored protein), did not partition into GEM domains in the Golgi complex and trafficked from TGN to plasma membrane by a brefeldin A-insensitive exocytic pathway. Moreover, a dominant negative form of Rab11, which prevents exit of vesicular stomatitis virus glycoprotein from the Golgi complex, did not influence the capacity of GD3 to reach the cell surface. Our results strongly support the notion that most ganglioside GD3 traffics from the TGN to the plasma membrane by a non-conventional vesicular pathway where lateral membrane segregation of vesicular stomatitis virus glycoprotein (non-GEM resident) and glycosylphosphatidylinositol-anchored proteins (GEM resident) from GD3 is required before exiting TGN.

Received for publication, June 25, 2004 , and in revised form, August 9, 2004.

^* This work was supported in part by grants from Secretaría de Ciencia y Tecnología-Universidad Nacional de Córdoba, International Society for Neurochemistry (Special ISN One-Time Fund), Proyectos de Estímulo a la Investigación of Consejo Nacional de Investigaciones Científicas y Técnicas Grant 6462, Fundación Antorchas Grant 14116-112, and from Programa de Centros Asociados de Posgrado Brasil/Argentina (CAPES-SPU) Grant 001/02). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this article.

Recipient of the Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina) fellowship.

^¶ Recipient of Fundación Antorchas fellowships.

^|| Career Investigator of Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina). To whom correspondence should be addressed: CIQUIBIC (UNC-CONICET), Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, 5000 Córdoba, Argentina. Tel.: 54-351-4334171; Fax: 54-351-4334074; E-mail: daniotti{at}dqb.fcq.unc.edu.ar.

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