rab3‐Peptide stimulates exocytosis from mast cells via a pertussis toxin‐sensitive mechanism
- 25 October 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 333 (1-2) , 56-60
- https://doi.org/10.1016/0014-5793(93)80374-4
Abstract
Synthetic peptides of the putative effector domain of members of the rab3 gene family of small GTP-binding proteins have been shown to have potent actions on vesicular transport and exocytosis [1,2]. Here, we use similar rab3-effector domain peptides to study their role in intracellular signalling in mast cells. We find that rab3-like peptides stimulate exocytosis and decrease cyclic 3',5'-AMP levels in these cells when applied extracellularly. Cells pretreated with pertussis toxin (PtX) to selectively uncouple αi/α0 type G proteins from their biological activators, however, did not respond to rab3 peptides. rab3-like peptides also induce a Ca2+ transient in mast cells. These observations provide evidence for functional coupling between an effector domain peptide sequence of rab3 protein and a PtX-sensitive G protein substrate.Keywords
This publication has 14 references indexed in Scilit:
- Stimulation of exocytotic membrane fusion by modified peptides of the rab3 effector domain: re-evaluation of the role of rab3 in regulated exocytosisBiochemical Journal, 1993
- A Synthetic Peptide of the Effector Domain of rab3A Stimulates Inositol 1,4,5-Trisphosphate Production in Digitonin-Permeabilized Pancreatic AciniBiochemical and Biophysical Research Communications, 1993
- Synthetic peptides of the rab3 effector domain stimulate a membrane fusion event involved in regulated exocytosisFEBS Letters, 1993
- Guanine nucleotide is essential and Ca2+ is a modulator in the exocytotic reaction of permeabilized rat mast cellsBiochemical Journal, 1992
- Exocytotic fusion is activated by Rab3a peptidesNature, 1992
- Synthetic peptides of the effector‐binding domain of rab enhance secretion from digitonin‐permeabilized chromaffin cellsFEBS Letters, 1992
- A synthetic peptide of the rab3a effector domain stimulates amylase release from permeabilized pancreatic acini.Proceedings of the National Academy of Sciences, 1992
- Interaction of mastoparan with the low molecular mass GTP‐binding proteins rho/racFEBS Letters, 1991
- Neomycin is a potent secretagogue of mast cells that directly activates a GTP-binding protein involved in exocytosis.The Journal of cell biology, 1990
- G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptidesTrends in Pharmacological Sciences, 1990