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M109601200v1
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Papers In Press, published online ahead of print January 7, 2002
J. Biol. Chem, 10.1074/jbc.M109601200
Submitted on October 4, 2001
Revised on December 28, 2001
Accepted on January 3, 2002

Association of GM3 with Zap-70 induced by T cell activation in plasma membrane microdomains. GM3 as a marker of microdomains in human lymphocytes

Tina Garofalo, Luisa Lenti, Agostina Longo, Roberta Misasi, Vincenzo Mattei, Giuseppe M Pontieri, Antonio Pavan, and Maurizio Sorice

Dipartimento di Medicina Sperimentale e Patologia, Università di Roma La Sapienza, Roma 00161

Corresponding Author: maurizio.sorice{at}uniroma1.it

Recent evidence demonstrated that T cell activation leads to the redistribution of membrane and intracellular kinase-rich raft microdomains at the site of TCR engagement. In this investigation we demonstrate that GM3 is the main ganglioside constituent of these microdomains in human lymphocytes, by high performance thin layer chromatography, gas chromatographic and mass spectrometric analyses. Then, we analyzed GM3 distribution and its interaction with the phosphorylation protein Zap-70. Human T lymphocytes were stimulated with anti-CD3 and anti-CD28. Immunofluorescence microscopy analysis revealed a clustered GM3 distribution over the cell surface and an intracellular localization, resembling specific cytoplasmic compartment(s). Scanning confocal microscopy showed that T cell activation induced a significant association between GM3 and Zap-70, as revealed by nearly complete colocalization areas; very few colocalization areas were detected in unstimulated cells. Coimmunoprecipitation experiments revealed that GM3 was immunoprecipitated by anti-Zap-70 only after costimulation through CD3 and CD28, as detected by both thin layer chromatography and immunoblotting. Therefore, T cell activation does not promote a redistribution of GEM, but induces Zap-70 translocation in selective membrane domains in which Zap-70 may interact with GM3. This suggests that GM3 is a component of a multimolecular signaling complex involved in T cell activation.


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