scholarly journals SLP-76 IS REQUIRED FOR TCR SIGNAL TRANSDUCTION IN PRIMARY T LYMPHOCYTES.

2006 ◽  
Vol 82 (Suppl 2) ◽  
pp. 1025-1026
Author(s):  
&NA;
2003 ◽  
Vol 75 (2) ◽  
pp. 373-381 ◽  
Author(s):  
Anis Larbi ◽  
Nadine Douziech ◽  
Gilles Dupuis ◽  
Abdelouahed Khalil ◽  
Hugues Pelletier ◽  
...  

1995 ◽  
Vol 92 (21) ◽  
pp. 9810-9814 ◽  
Author(s):  
L. J. Holsinger ◽  
D. M. Spencer ◽  
D. J. Austin ◽  
S. L. Schreiber ◽  
G. R. Crabtree

2000 ◽  
Vol 151 (2) ◽  
pp. 199-208 ◽  
Author(s):  
Thomas Harder ◽  
Marina Kuhn

Activation of T cell antigen receptor (TCR) induces tyrosine phosphorylations that mediate the assembly of signaling protein complexes. Moreover, cholesterol-sphingolipid raft membrane domains have been implicated to play a role in TCR signal transduction. Here, we studied the assembly of TCR with signal transduction proteins and raft markers in plasma membrane subdomains of Jurkat T leukemic cells. We employed a novel method to immunoisolate plasma membrane subfragments that were highly concentrated in activated TCR–CD3 complexes and associated signaling proteins. We found that the raft transmembrane protein linker for activation of T cells (LAT), but not a palmitoylation-deficient non-raft LAT mutant, strongly accumulated in TCR-enriched immunoisolates in a tyrosine phosphorylation–dependent manner. In contrast, other raft-associated molecules, including protein tyrosine kinases Lck and Fyn, GM1, and cholesterol, were not highly concentrated in TCR-enriched plasma membrane immunoisolates. Many downstream signaling proteins coisolated with the TCR/LAT-enriched plasma membrane fragments, suggesting that LAT/TCR assemblies form a structural scaffold for TCR signal transduction proteins. Our results indicate that TCR signaling assemblies in plasma membrane subdomains, rather than generally concentrating raft-associated membrane proteins and lipids, form by a selective protein-mediated anchoring of the raft membrane protein LAT in vicinity of TCR.


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