PMID- 10209036
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 189
IP  - 8
DP  - 1999 Apr 19
TI  - SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked
      dimer regulating human T cell activation.
PG  - 1181-94
AB  - 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.
FAU - Marie-Cardine, A
AU  - Marie-Cardine A
AD  - Immunomodulation Laboratory of the Institute for Immunology, University of
      Heidelberg, 69120 Heidelberg, Germany.
FAU - Kirchgessner, H
AU  - Kirchgessner H
FAU - Bruyns, E
AU  - Bruyns E
FAU - Shevchenko, A
AU  - Shevchenko A
FAU - Mann, M
AU  - Mann M
FAU - Autschbach, F
AU  - Autschbach F
FAU - Ratnofsky, S
AU  - Ratnofsky S
FAU - Meuer, S
AU  - Meuer S
FAU - Schraven, B
AU  - Schraven B
LA  - eng
SI  - GENBANK/AJ010059
SI  - GENBANK/AJ236881
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Disulfides)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (NFATC Transcription Factors)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phorbol Esters)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Antigen, T-Cell)
RN  - 0 (SIT1 protein, human)
RN  - 0 (Transcription Factors)
RN  - EC 3.1.3.48 (PTPN11 protein, human)
RN  - EC 3.1.3.48 (PTPN6 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (SH2 Domain-Containing Protein Tyrosine Phosphatases)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Carrier Proteins/chemistry/*genetics
MH  - Cloning, Molecular
MH  - DNA-Binding Proteins/metabolism
MH  - Dimerization
MH  - Disulfides/chemistry
MH  - Gene Expression Regulation/genetics
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Jurkat Cells
MH  - Lymphocyte Activation
MH  - Membrane Glycoproteins/chemistry/*genetics
MH  - Membrane Proteins/chemistry/*genetics
MH  - Molecular Sequence Data
MH  - NFATC Transcription Factors
MH  - *Nuclear Proteins
MH  - Phorbol Esters/pharmacology
MH  - Phosphorylation
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 11
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - RNA, Messenger/metabolism
MH  - Receptors, Antigen, T-Cell/metabolism
MH  - SH2 Domain-Containing Protein Tyrosine Phosphatases
MH  - Sequence Alignment
MH  - Signal Transduction/genetics
MH  - T-Lymphocytes/*metabolism
MH  - Transcription Factors/metabolism
MH  - src Homology Domains/genetics
PMC - PMC2193021
EDAT- 1999/04/20 00:00
MHDA- 1999/04/20 00:01
CRDT- 1999/04/20 00:00
PHST- 1999/04/20 00:00 [pubmed]
PHST- 1999/04/20 00:01 [medline]
PHST- 1999/04/20 00:00 [entrez]
AID - 10.1084/jem.189.8.1181 [doi]
PST - ppublish
SO  - J Exp Med. 1999 Apr 19;189(8):1181-94. doi: 10.1084/jem.189.8.1181.