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Published 6 January 2003. doi:10.1083/jcb.200207096
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© The Rockefeller University Press, 0021-9525/2003/1/125 $5.00
The Journal of Cell Biology, Volume 160, Number 1, 125-135

Article

Dynamic changes in the mobility of LAT in aggregated lipid rafts upon T cell activation



Natsuko Tanimura1, Masakazu Nagafuku1, Yasuko Minaki1, Yukio Umeda3, Fumie Hayashi1, Junko Sakakura1, Akiko Kato1, Douglas R. Liddicoat1, Masato Ogata2, Toshiyuki Hamaoka2 and Atsushi Kosugi1,4

1 School of Allied Health Sciences, Faculty of Medicine
2 Department of Oncogenesis, Graduate School of Medicine (C6), Osaka University, Suita, Osaka 565-0871, Japan
3 First Department of Surgery, Gifu University School of Medicine, Gifu, 500-8705, Japan
4 Core Research for Evaluational Science and Technology program (CREST), Japan Science and Technology Corporation (JST), Saitama, 332-0012 Japan

Address correspondence to Atsushi Kosugi, School of Allied Health Sciences, Faculty of Medicine, Osaka University, 1-7, Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-2599. Fax: 81-6-6879-2599. E-mail: kosugi{at}sahs.med.osaka-u.ac.jp

Lipid rafts are known to aggregate in response to various stimuli. By way of raft aggregation after stimulation, signaling molecules in rafts accumulate and interact so that the signal received at a given membrane receptor is amplified efficiently from the site of aggregation. To elucidate the process of lipid raft aggregation during T cell activation, we analyzed the dynamic changes of a raft-associated protein, linker for activation of T cells (LAT), on T cell receptor stimulation using LAT fused to GFP (LAT-GFP). When transfectants expressing LAT-GFP were stimulated with anti-CD3–coated beads, LAT-GFP aggregated and formed patches at the area of bead contact. Photobleaching experiments using live cells revealed that LAT-GFP in patches was markedly less mobile than that in nonpatched regions. The decreased mobility in patches was dependent on raft organization supported by membrane cholesterol and signaling molecule binding sites, especially the phospholipase C{gamma}1 binding site in the cytoplasmic domain of LAT. Thus, although LAT normally moves rapidly at the plasma membrane, it loses its mobility and becomes stably associated with aggregated rafts to ensure organized and sustained signal transduction required for T cell activation.

Key Words: raft aggregation; signal transduction; T cell receptor; linker for activation of T cells; photobleaching


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