Evidence for inducible recruitment of Wiskott-Aldrich syndrome protein to T cell receptor-CD3 complex in Jurkat T cells

Author(s):  
Pussadee Paensuwan
FEBS Journal ◽  
2005 ◽  
Vol 272 (23) ◽  
pp. 6131-6144 ◽  
Author(s):  
Mitsuru Sato ◽  
Ryo Iwaya ◽  
Kazumasa Ogihara ◽  
Ryoko Sawahata ◽  
Hiroshi Kitani ◽  
...  

2007 ◽  
Vol 104 (51) ◽  
pp. 20296-20301 ◽  
Author(s):  
Y. Kaizuka ◽  
A. D. Douglass ◽  
R. Varma ◽  
M. L. Dustin ◽  
R. D. Vale

2000 ◽  
Vol 149 (1) ◽  
pp. 181-194 ◽  
Author(s):  
Matthias Krause ◽  
Antonio S. Sechi ◽  
Marlies Konradt ◽  
David Monner ◽  
Frank B. Gertler ◽  
...  

T cell receptor (TCR)-driven activation of helper T cells induces a rapid polarization of their cytoskeleton towards bound antigen presenting cells (APCs). We have identified the Fyn- and SLP-76–associated protein Fyb/SLAP as a new ligand for Ena/ vasodilator-stimulated phosphoprotein (VASP) homology 1 (EVH1) domains. Upon TCR engagement, Fyb/SLAP localizes at the interface between T cells and anti-CD3–coated beads, where Evl, a member of the Ena/VASP family, Wiskott-Aldrich syndrome protein (WASP) and the Arp2/3 complex are also found. In addition, Fyb/SLAP is restricted to lamellipodia of spreading platelets. In activated T cells, Fyb/SLAP associates with Ena/VASP family proteins and is present within biochemical complexes containing WASP, Nck, and SLP-76. Inhibition of binding between Fyb/SLAP and Ena/VASP proteins or WASP and the Arp2/3 complex impairs TCR-dependent actin rearrangement, suggesting that these interactions play a key role in linking T cell signaling to remodeling of the actin cytoskeleton.


2014 ◽  
Vol 18 (1) ◽  
pp. 73 ◽  
Author(s):  
Yun-Jung Lee ◽  
Tae Joon Won ◽  
Kyeong Eun Hyung ◽  
Mi Ji Lee ◽  
Young-hye Moon ◽  
...  

2004 ◽  
Vol 4 (4) ◽  
pp. 301-308 ◽  
Author(s):  
Robert T. Abraham ◽  
Arthur Weiss

1998 ◽  
Vol 20 (11) ◽  
pp. 551-563 ◽  
Author(s):  
Margaret M. Harnett ◽  
Maureen R. Deehan ◽  
Denise M. Williams ◽  
William Harnett

2001 ◽  
Vol 193 (11) ◽  
pp. 1269-1284 ◽  
Author(s):  
Henning Kirchgessner ◽  
Jes Dietrich ◽  
Jeanette Scherer ◽  
Pia Isomäki ◽  
Vladimir Korinek ◽  
...  

T cell receptor (TCR)-interacting molecule (TRIM) is a recently identified transmembrane adaptor protein, which is exclusively expressed in T cells. Here we demonstrate that in mature T cells, TRIM preferentially interacts with the TCR via the TCR-ζ chains and to a lesser extent via the CD3-ε/γ heterodimer. Transient or stable overexpression of TRIM in Jurkat T cells results in enhancement of TCR expression on the cell surface and elevated induction of Ca2+ mobilization after T cell activation. TRIM-mediated upregulation of TCR expression results from inhibition of spontaneous TCR internalization and stabilization of TCR complexes on the cell surface. Collectively, our data identify TRIM as a novel integral component of the TCR complex and suggest that one function of TRIM might be to modulate the strength of signals transduced through the TCR through regulation of TCR expression on the cell surface.


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