Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling.

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  • Author(s): Lafont F;Lafont F; Simons K
  • Source:
    Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2001 Mar 13; Vol. 98 (6), pp. 3180-4.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Print ISSN: 0027-8424 (Print) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : National Academy of Sciences
    • Subject Terms:
      Signal Transduction* ; Ubiquitin-Protein Ligases*; Calcium-Binding Proteins/*metabolism ; Ligases/*metabolism ; Membrane Microdomains/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Receptors, IgE/*metabolism; Animals ; Calcium-Binding Proteins/genetics ; Endosomal Sorting Complexes Required for Transport ; Immunoglobulin E/metabolism ; Immunoglobulin E/pharmacology ; Ligases/genetics ; Nedd4 Ubiquitin Protein Ligases ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-cbl ; Rats ; Tumor Cells, Cultured ; Ubiquitin/metabolism
    • Abstract:
      The high affinity receptor for IgE, FcepsilonRI on mast cells and basophils plays an essential role in immunological defense. Upon multivalent antigen binding, FcepsilonRI becomes phoshorylated by the protein-tyrosine kinase Lyn, as a result of receptor clustering in lipid rafts. FcepsilonRI has been shown to be ubiquitinated. Ubiquitination can lead to degradation by proteasomes, but it can also act as a sorting signal to internalize proteins destined to the endosomal/lysosomal pathway. We have analyzed whether FcepsilonRI ubiquitination takes place within rafts. We report biochemical and imaging evidence in rat basoleukemia cells for the presence of ubiquitinated FcepsilonRI in clustered rafts upon receptor activation. Moreover, we demonstrated that the ubiquitin ligases Cbl and Nedd4 colocalize with FcepsilonRI patches and showed that both ligases become associated with lipid rafts after activation of IgE signaling. Because Cbl is known to interact with the FcepsilonRI signaling complex, ubiquitination is likely to be an important parameter regulating IgE-triggered signaling occurring in rafts.
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    • Accession Number:
      0 (Calcium-Binding Proteins)
      0 (Endosomal Sorting Complexes Required for Transport)
      0 (Proto-Oncogene Proteins)
      0 (Receptors, IgE)
      0 (Ubiquitin)
      37341-29-0 (Immunoglobulin E)
      EC 2.3.2.26 (NEDD4L protein, rat)
      EC 2.3.2.26 (Nedd4 Ubiquitin Protein Ligases)
      EC 2.3.2.26 (Nedd4 protein, rat)
      EC 2.3.2.27 (Proto-Oncogene Proteins c-cbl)
      EC 2.3.2.27 (Ubiquitin-Protein Ligases)
      EC 6.- (Ligases)
    • Publication Date:
      Date Created: 20010315 Date Completed: 20011204 Latest Revision: 20181113
    • Publication Date:
      20221213
    • Accession Number:
      PMC30627
    • Accession Number:
      10.1073/pnas.051003498
    • Accession Number:
      11248052