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Structural and functional evidence that Nck interaction with CD3epsilon regulates T-cell receptor activity.

Abstract：

:Recruitment of signaling molecules to the cytoplasmic domains of the CD3 subunits of the T-cell receptor (TCR) is crucial for early T-cell activation. These transient associations either do or do not require tyrosine phosphorylation of CD3 immune tyrosine activation motifs (ITAMs). Here we show that the non-ITAM-requiring adaptor protein Nck forms a complex with an atypical PxxDY motif of the CD3epsilon tail, which encompasses Tyr166 within the ITAM and a TCR endocytosis signal. As suggested by the structure of the complex, we find that Nck binding inhibits phosphorylation of the CD3epsilon ITAM by Fyn and Lck kinases in vitro. Moreover, the CD3epsilon-Nck interaction downregulates TCR surface expression upon physiological stimulation in mouse primary lymph node cells. This indicates that Nck performs an important regulatory function in T lymphocytes by inhibiting ITAM phosphorylation and/or removing cell surface TCR via CD3epsilon interaction.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Takeuchi K,Yang H,Ng E,Park SY,Sun ZY,Reinherz EL,Wagner G

doi

10.1016/j.jmb.2008.05.037

subject

Has Abstract

pub_date

2008-07-18 00:00:00

pages

704-16

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(08)00603-7

journal_volume

380

pub_type

杂志文章

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