FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation.

The human IL-4 receptor contains a sequence (the 14R motif) centered on Y497 that, when phosphorylated, interacts with phosphotyrosine-binding (PTB) domain proteins. Here, we describe a PTB domain protein, FRIP, that is phosphorylated in response to cytokine stimulation. FRIP is related to the rasGAP-associated protein p62dok and is bound by ...
the N-terminal SH2 domain of rasGAP. The frip gene maps to the hairless (hr) locus on mouse chromosome 14. hr/hr mice exhibit lymphadenopathy, and their lymph node T cells proliferate more vigorously to anti-CD3 with IL-4 or IL-2 stimulation than +/hr T cells. FRIP expression is significantly reduced in T cells from hr/hr mice. FRIP may negatively regulate proliferation by acting as an adapter molecule between rasGAP and receptor complexes.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, CD4-Positive T-Lymphocytes, Cell Line, Cell Line, Transformed, Cells, Cultured, Chromosome Mapping, DNA, Complementary, DNA-Binding Proteins, Female, GTPase-Activating Proteins, Humans, Interleukin-2, Interleukin-3, Interleukin-4, Male, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Phosphotyrosine, Proteins, RNA, Messenger, RNA-Binding Proteins, Receptors, Interleukin-4, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Tissue Distribution, Transcription Factors
Immunity
Date: Jul. 01, 1998
Download Curated Data For This Publication
120726
Switch View:
  • Interactions 1