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Originally published In Press as doi:10.1074/jbc.M110515200 on May 14, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26252-26259, July 19, 2002
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A Close Association of the Ganglioside-specific Sialidase Neu3 with Caveolin in Membrane Microdomains*

Yan WangDagger §, Kazunori YamaguchiDagger , Tadashi WadaDagger , Keiko HataDagger , Xuejian Zhao§, Toyoshi Fujimoto, and Taeko MiyagiDagger ||

From the Dagger  Division of Biochemistry, Research Institute, Miyagi Prefectural Cancer Center, Natori, Miyagi 981-1293, Japan, the § Laboratory of Reproductive Pathophysiology, Jilin University of Medical Sciences, Changchun 130021, The Peoples Republic of China, and the  Department of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan

The ganglioside-specific sialidase Neu3 has been suggested to play essential roles in regulation of cell surface functions because of its major localization in the plasma membrane and strict substrate preference for gangliosides involved in signal transduction. Here we show that human Neu3 sialidase is enriched in caveolae microdomains and closely associates with caveolin like other caveolin-binding signaling molecules. Using HeLa cells and Neu3-transfected COS-1 cells, endogenous and exogenous Neu3 was found to co-concentrate caveolin-1 in low density Triton X-100-insoluble membrane fractions on sucrose density gradients of the respective cell extracts, as assessed by enzyme activity assays and immunoblotting with a monoclonal antibody to human Neu3. The presence of a putative caveolin-binding motif within Neu3 prompted us to determine whether Neu3 binds to caveolin-1. In transfectants expressing a polyhistidine-tagged form of Neu3, caveolin-1 co-eluted with Neu3 on affinity column chromatography. A mutation with a single amino acid change in the caveolin-binding motif led to inhibition of recruitment of the sialidase to the microdomain, accompanied by reduction of the enzyme activity. Neu3 also failed to associate with caveolin-enriched microdomains by cholesterol depletion with beta -cyclodextrin (with concomitant decrease of the sialidase activity), whereas Neu3 was activated by increased caveolin-1 expression. The tight association of Neu3 with caveolin-1 was supported further by co-immunoprecipitation of Neu3 by anti-caveolin-1 antibody. These results strongly suggest that Neu3 functions as a caveolin-related signaling molecule within caveolin-rich microdomains.

* This study was supported in part by grants-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Science, Sports, Culture, and Technology of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed. Tel.: 81-22-384-3151; Fax: 81-22-381-1195; E-mail: tmiyagi@mcc.pref.miyagi.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.