The type III inositol 1,4,5-trisphosphate receptor is phosphorylated by cAMP-dependent protein kinase at three sites
Open accessAbstract
IP3 (inositol 1,4,5-trisphosphate) receptors form tetrameric, IP3-gated Ca2+ channels in endoplasmic reticulum membranes, and are substrates for several kinases, including PKA (cAMP-dependent protein kinase). Activation of PKA has been reported to either enhance or inhibit type III IP3 receptor Ca2+-channel activity, but, as yet, the sites of phosphorylation remain unknown. Here, we reveal that PKA phosphorylates the type III IP3 receptor at Ser916, Ser934 and Ser1832, and that, intriguingly, each site is located close to a putative surface-exposed peptide loop. Furthermore, we demonstrate that Ser934 is considerably more susceptible to PKA-dependent phoshorylation than either Ser916 or Ser1832. These findings define the sites at which the type III IP3 receptor is phosphorylated by PKA, and provide the basis for exploring the functional consequences of this regulatory event.
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cAMP-PKA signalling can stimulate phosphorylation of InsP3 receptors, promoting InsP3-mediated Ca2+ release.
“For example, cAMP–PKA signalling can stimulate the phosphorylation of InsP3 receptors, which promotes InsP3-mediated Ca2+ release97.”
From Stress signalling pathways that impair prefrontal cortex structure and function (2009) · cites this paper as [97]
The Conclusions report that PKA phosphorylates type III InsP3 receptors. The Introduction says phosphorylation appears to enhance type I receptor Ca2+ channel activity, but reports both stimulatory and inhibitory findings for type III receptors. Thus the source supports a possible increase in Ca2+ release, not an unqualified promoting effect across InsP3 receptors. (LLM, conf=0.84)
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- Yamada, N., Makino, Y., Clark, R. A., Pearson, D. W., Mattei, M. G., Guenet, J. L., Ohama, E., Fujino, I., Miyawaki, A., Furuichi, T. and Mikoshiba, K. (1994) Human inositol 1,4,5-trisphosphate receptor, InsP 3 R1: structure, function, regulation of expression and chromosomal location. Biochem. J. 302, 781-790
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Stress signalling pathways that impair prefrontal cortex structure and function
Arnsten, A. F. T. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2648 · Cited by 3,299 · see citing works
Arnsten, A. F. T., Wang, M. J., & Paspalas, C. D. (2012) · Neuron · doi:10.1016/j.neuron.2012.08.038 · Cited by 538 · see citing works
Hains, A. B., Vu, M. A. T., Maciejewski, P. K., van Dyck, C. H., Gottron, M., & Arnsten, A. F. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908563106 · Cited by 234 · see citing works
cAMP-PKA phosphorylation of tau confers risk for degeneration in aging association cortex
Carlyle, B. C., Nairn, A. C., Wang, M., Yang, Y., Jin, L. E., Simen, A. A., Ramos, B. P., Bordner, K. A., Craft, G. E., Davies, P., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322360111 · Cited by 139 · see citing works
Temporal Sensitivity of Protein Kinase A Activation in Late-Phase Long Term Potentiation
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- Authors
- Soulsby, M. D., & Wojcikiewicz, R. J. H.
- Affiliations
- SUNY Upstate Medical University (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2005-12-06
- Volume
- 392
- Issue
- 3
- Pages
- 493-497
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1316288
- OpenAlex
- W2047663792
- Cited by
- 71
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 8 · 2021: 3 · 2019: 4 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 2 · 2012: 4
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (0256225T)
- National Institutes of Health (DK49194)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 49194, R29DK049194, R01DK049194)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- IP3 receptor, protein kinase A, protein phosphorylation, phosphorylation sites, endoplasmic reticulum, receptor regulation
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Humans, Molecular Sequence Data, Phosphorylation, Calcium Channels, Sequence Homology, Amino Acid, Cyclic AMP-Dependent Protein Kinases, Receptors, Cytoplasmic and Nuclear, Calcium Signaling, Mice, Rats, Inositol 1,4,5-Trisphosphate Receptors
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