Abstract
Hrs binding protein (Hbp) tightly associated with Hrs is thought to play a regulatory role in vesicular trafficking during endocytosis and exocytosis. In this study, we have expressed dominant-negative mutants of Hbp to evaluate their effects on the degranulation of secretory granules in RBL-2H3 mast cells. The dominant-negative mutants of Hbp significantly inhibited IgE receptor (FcϵRI)-triggered secretory response as tested by β-hexosaminidase release. These results suggest that Hbp functions as a regulator in the FcϵRI-triggered degranulation of secretory granules in mast cells.
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