Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein) (Q24291394)

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English	Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)	scientific article

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scholarly article

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Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein) (English)

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transmembrane protein

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Signaling threshold regulating transmembrane adaptor 1

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GOA release 2020-03-11

SH2 domain binding

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GOA release 2020-03-11

author name string

K I Pfrepper

1

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A Marie-Cardine

2

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L Simeoni

3

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Y Kuramitsu

4

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A Leo

5

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J Spicka

6

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I Hilgert

7

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J Scherer

8

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B Schraven

9

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language of work or name

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publication date

June 2001

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European Journal of Immunology

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31

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6

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1825-36

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T cell antigen-receptor signal transduction

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The role of membrane-associated adaptors in T cell receptor signalling

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Integration of receptor-mediated signals in T cells by transmembrane adaptor proteins

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Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells

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LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation

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LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway

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Identification of a novel dimeric phosphoprotein (PP29/30) associated with signaling receptors in human T lymphocytes and natural killer cells

1 reference

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SH2 domains recognize specific phosphopeptide sequences

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The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells

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Identifiers

10.1002/1521-4141(200106)31:6<1825::AID-IMMU1825>3.0.CO;2-V

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release_6zxgg6x6ina6vfm5h7fjtt64ki

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