Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule

J Biol Chem. 1996 Oct 11;271(41):25569-74. doi: 10.1074/jbc.271.41.25569.

Abstract

BIT (a brain immunoglobulin-like molecule with tyrosine-based activation motifs) is a brain-specific membrane protein which has two cytoplasmic TAMs (tyrosine-based activation motifs). Using the Far Western blotting technique, we detected association of a 70-kDa protein with the tyrosine-phosphorylated TAMs of BIT. A mouse brain cDNA library in lambdagt11 was screened for this association, and two positive clones encoding tyrosine phosphatase SH-PTP2 were isolated. SH-PTP2 has two SH2 domains and is believed to function as a positive mediator in receptor tyrosine kinase signaling. SH-PTP2 and BIT were coimmunoprecipitated from phosphorylated rat brain lysate, and BIT was a major tyrosine-phosphorylated protein associated with SH-PTP2 in this lysate. This interaction was also observed in Jurkat T cells transfected with BIT cDNA depending on tyrosine phosphorylation of BIT. Bisphosphotyrosyl peptides corresponding to BIT-TAMs stimulated SH-PTP2 activity 33-35-fold in vitro, indicating that two SH2 domains of SH-PTP2 simultaneously interact with two phosphotyrosines of BIT-TAM. Our findings suggest that the tyrosine phosphorylation of BIT results in stimulation of the signal transduction pathway promoted by SH-PTP2 and that BIT is probably a major receptor molecule in the brain located just upstream of SH-PTP2.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Western
  • Brain / metabolism*
  • Cell Line
  • DNA Primers
  • Enzyme Activation
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Models, Structural
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / isolation & purification
  • Nerve Tissue Proteins / metabolism*
  • Peptide Fragments / chemistry
  • Phosphopeptides / chemical synthesis
  • Phosphopeptides / chemistry
  • Phosphorylation
  • Polymerase Chain Reaction
  • Protein Conformation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / metabolism*
  • Rats
  • Receptors, Antigen / chemistry
  • Receptors, Antigen / isolation & purification
  • Receptors, Antigen / metabolism*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction
  • Transfection
  • Tyrosine*

Substances

  • DNA Primers
  • Intracellular Signaling Peptides and Proteins
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Phosphopeptides
  • Receptors, Antigen
  • Recombinant Fusion Proteins
  • Tyrosine
  • PTPN11 protein, human
  • PTPN6 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6
  • Protein Tyrosine Phosphatases
  • Ptpn11 protein, mouse
  • Ptpn11 protein, rat
  • Ptpn6 protein, mouse
  • Ptpn6 protein, rat

Associated data

  • GENBANK/D38468
  • GENBANK/D84372