High impact information on Fcer1g

• This could be particularly relevant to other multimeric receptors containing Fc epsilon RI gamma-chains or the related zeta and eta chains such as the T-cell antigen receptor (TCR) and the low-affinity receptor for immunoglobulin G (Fc gamma RIII, CD16) [1].
• Association of p72syk with the tyrosine phosphorylated Fc epsilon RI gamma chain was detected only after receptor aggregation [2].
• In an effort to determine the function of Fc epsilon RI-gamma, we used chimeric proteins containing the extracellular and transmembrane domains of the alpha chain of the human interleukin 2 receptor (Tac) and the cytoplasmic domains of either T cell receptor-zeta or Fc epsilon RI-gamma [3].
• Signal transduction by the cytoplasmic domains of Fc epsilon RI-gamma and TCR-zeta in rat basophilic leukemia cells [3].
• The high affinity Fc epsilon receptor gamma subunit (Fc epsilon RI gamma) facilitates T cell receptor expression and antigen/major histocompatibility complex-driven signaling in the absence of CD3 zeta and CD3 eta [4].

Biological context of Fcer1g

• To identify the functional significance of sequence homologies between CD3 zeta and Fc epsilon RI gamma in T cells, we have transfected a Fc epsilon RI gamma cDNA into a T cell hybridoma lacking CD3 zeta and CD3 eta proteins [4].
• Transfection of the cloned Fc epsilon RI gamma subunit into the variant cells restored the surface expression of Fc epsilon RI and responsiveness to both the antigen and anti-Fc epsilon RI mAb but had no effect on responsiveness to anti-Thy-1 mAb [5].
• In this paper we describe the search for other activation-associated tyrosine kinases by the ability to phosphorylate a cytoplasmic domain peptide of the Fc epsilon RI gamma-subunit [6].

Regulatory relationships of Fcer1g

• The combined data indicate that aggregation of surface Thy-1 glycoproteins activates a metabolic pathway which is independent of the presence of Fc epsilon RI gamma subunit and surface expression of Fc epsilon RI [5].

Other interactions of Fcer1g

• A TCR composed of Ti alpha-beta CD3 gamma delta epsilon Fc epsilon RI gamma-gamma is sufficient to restore the coupling of TCR antigen recognition to the interleukin-2 induction pathway, demonstrating the functional significance of structural homology between the above receptor subunits [4].

References