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Cell surface control of the multiubiquitination and deubiquitination of high‐affinity immunoglobulin E receptors.
Author(s) -
Paolini R.,
Kinet J.P.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05712.x
Subject(s) - biology , receptor , antibody , microbiology and biotechnology , cell surface receptor , surface immunoglobulin , biochemistry , immunology , b cell
Multiubiquitination of proteins is a critical step leading to selective degradation for many polypeptides. Therefore, activation‐induced multiubiquitination of cell surface receptors, such as the platelet‐derived growth factor (PDGF) receptor and the T cell antigen (TCR) receptor, may correspond to a degradation pathway for ligand‐receptor complexes. Here we show that the antigen‐induced engagement of high‐affinity immunoglobulin E receptors (Fc epsilon RI) results in the immediate multiubiquitination of Fc epsilon RI beta and gamma chains. This ubiquitination is independent of receptor phosphorylation and is restricted to activated receptors. Surprisingly, receptor multiubiquitination is immediately reversible when receptors are disengaged. Therefore, multiubiquitination and deubiquitination of Fc epsilon RI receptors is controlled at the cell surface by receptor engagement and disengagement. The rapidity, specificity and, most importantly, the reversibility of the activation‐induced receptor multiubiquitination suggest that this process may turn on/off a cell surface receptor signaling function thus far unsuspected.