[HTML][HTML] Wasp recruitment to the T cell: APC contact site occurs independently of Cdc42 activation
JL Cannon, CM Labno, G Bosco, A Seth… - Immunity, 2001 - cell.com
Cdc42 and WASP are critical regulators of actin polymerization whose function during T cell
signaling is poorly understood. Using a novel reagent that specifically detects Cdc42-GTP in
fixed cells, we found that activated Cdc42 localizes to the T cell: APC contact site in an
antigen-dependent manner. TCR signaling alone was sufficient to induce localization of
Cdc42-GTP, and functional Lck and Zap-70 kinases were required. WASP also localized to
the T cell: APC contact site in an antigen-dependent manner. Surprisingly, WASP …
signaling is poorly understood. Using a novel reagent that specifically detects Cdc42-GTP in
fixed cells, we found that activated Cdc42 localizes to the T cell: APC contact site in an
antigen-dependent manner. TCR signaling alone was sufficient to induce localization of
Cdc42-GTP, and functional Lck and Zap-70 kinases were required. WASP also localized to
the T cell: APC contact site in an antigen-dependent manner. Surprisingly, WASP …
Abstract
Cdc42 and WASP are critical regulators of actin polymerization whose function during T cell signaling is poorly understood. Using a novel reagent that specifically detects Cdc42-GTP in fixed cells, we found that activated Cdc42 localizes to the T cell:APC contact site in an antigen-dependent manner. TCR signaling alone was sufficient to induce localization of Cdc42-GTP, and functional Lck and Zap-70 kinases were required. WASP also localized to the T cell:APC contact site in an antigen-dependent manner. Surprisingly, WASP localization was independent of the Cdc42 binding domain but required the proline-rich domain. Our results indicate that localized WASP activation requires the integration of multiple signals: WASP is recruited via interaction with SH3 domain-containing proteins and is activated by Cdc42-GTP concentrated at the same site.
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