Title :
SHP2-interacting transmembrane adaptor protein (
SIT ), a novel disulfide-linked
dimer regulating human T cell activation
Abstract :
- T lymphocytes express several low molecular weight transmembrane adaptor proteins that recruit src homology (SH)2 domain-containing intracellular molecules to the cell membrane via tyrosine-based signaling motifs
- We describe here a novel molecule of this group termed SIT ( SHP2 interacting transmembrane adaptor protein )
- SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes
- After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase SHP2 via an immunoreceptor tyrosine-based inhibition motif
- Overexpression of SIT in Jurkat cells downmodulates T cell receptor- and phytohemagglutinin-mediated activation of the nuclear factor of activated T cells (NF-AT) by interfering with signaling processes that are probably located upstream of activation of phospholipase C. However, binding of SHP2 to SIT is not required for inhibition of NF-AT induction, suggesting that SIT not only regulates NF-AT activity but also controls NF-AT unrelated pathways of T cell activation involving SHP2
Output (sent_index, trigger,
protein,
sugar,
site):
- 3. glycoprotein, , SIT, -, -
- 3. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):