The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
PKA-Dependent and PKA-Independent Pathways for cAMP-Regulated Exocytosis
Abstract
Stimulus-secretion coupling is an essential process in secretory cells in which regulated exocytosis occurs, including neuronal, neuroendocrine, endocrine, and exocrine cells. While an increase in intracellular Ca 2+concentration ([Ca 2+]i) is the principal signal, other intracellular signals also are important in regulated exocytosis. In particular, the cAMP signaling system is well known to regulate and modulate exocytosis in a variety of secretory cells. Until recently, it was generally thought that the effects of cAMP in regulated exocytosis are mediated by activation of cAMP-dependent protein kinase (PKA), a major cAMP target, followed by phosphorylation of the relevant proteins. Although the involvement of PKA-independent mechanisms has been suggested in cAMP-regulated exocytosis by pharmacological approaches, the molecular mechanisms are unknown. Newly discovered cAMP-GEF/Epac, which belongs to the cAMP-binding protein family, exhibits guanine nucleotide exchange factor activities and exerts diverse effects on cellular functions including hormone/transmitter secretion, cell adhesion, and intracellular Ca 2+mobilization. cAMP-GEF/Epac mediates the PKA-independent effects on cAMP-regulated exocytosis. Thus cAMP regulates and modulates exocytosis by coordinating both PKA-dependent and PKA-independent mechanisms. Localization of cAMP within intracellular compartments (cAMP compartmentation or compartmentalization) may be a key mechanism underlying the distinct effects of cAMP in different domains of the cell.
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Metadata
- Authors
- Seino, S., & Shibasaki, T.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2005-10
- Volume
- 85
- Issue
- 4
- Pages
- 1303-1342
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2105100736
- Cited by
- 563
- References
- 39
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- closed
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