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Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J. and Yarden, Y. (2003) Endocytosis of receptor tyrosine kinases is driven by mono-, not poly-ubiquitylation. Journal of Biological Science, 278, 31323-31326.

has been cited by the following article:

• TITLE: The Cbl family of ubiquitin ligases regulates FcεRI expression and mast cell activation

  AUTHORS: Rosa Molfetta, Francesca Gasparrini, Angela Santoni, Rossella Paolini

  KEYWORDS: Mast Cells; Basophils; FcεRI; Negative Regulation; Cbl Proteins; Ubiquitination

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.12, December 23, 2013

  ABSTRACT: Antigen interaction with specific IgE bound to the high-affinity Fc receptor for IgE, constitutively expressed on the cell-surface of mast cells, generates signals that cause a shift in the resting state equilibrium of phosphorylation and dephosphorylation events that serves to maintain homeostasis. The outcome of this activated state is the release of a wide array of preformed and newly synthesized pro-inflammatory mediators. During the past few years, the existence of a negative feedback loop initiated upon FcεRI engagement has also been envisaged. This negative signal involves the coordinated action of adaptors, phosphatases and ubiquitin ligases that limits the intensity and duration of positive signals, thus modulating mast cell functions. Relevant to this, others and we have demonstrated that Cbl family proteins control the amplitude of FcεRI-generated signals by specific ubiquitin modification of activated receptor subunits and associated protein tyrosine kinases. In this article, we review advances in our understanding of the molecular mechanisms through which Cbl proteins regulate FcεRI expression and signaling.