The insulin secretory granule as a signaling hub
Abstract
The insulin granule was previously thought of as merely a container, but accumulating evidence suggests that it also acts as a signaling node. Regulatory pathways intersect at but also originate from the insulin granule membrane. Examples include the small G-proteins Rab3a and Rab27a, which influence granule movement, and the transmembrane proteins (tyrosine phosphatase receptors type N) PTPRN and PTPRN2, which upregulate β-cell transcription and proliferation. In addition, many cosecreted compounds possess regulatory functions, often related to energy metabolism. For instance, ATP and γ-amino butyric acid (GABA) modulate insulin and glucagon secretion, respectively; C-peptide protects β-cells and kidney cells; and amylin reduces gastric emptying and food intake via the brain. In this paper, we review the current knowledge of the insulin granule proteome and discuss its regulatory functions.
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The fractional release rates correspond to release rates of 0.04 granules/min, 1-2 granules/min and 0.5 granules/min.
“As a mouse β-cell contains ≈10,000 secretory granules (650), these values correspond to release rates of 0.04 granules/min, 1-2 granules/min and 0.5 granules/min (Figure 15A).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [650]
A mouse β-cell contains approximately 10,000 secretory granules.
“As a mouse β-cell contains ≈10,000 secretory granules (650), these values correspond to release rates of 0.04 granules/min, 1-2 granules/min and 0.5 granules/min (Figure 15A).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [650]
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Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793 · see citing works
Interactions between Muscle and Bone—Where Physics Meets Biology
Herrmann, M., Engelke, K., Ebert, R., Müller-Deubert, S., Rudert, M., Ziouti, F., Jundt, F., Felsenberg, D., & Jakob, F. (2020) · Biomolecules · doi:10.3390/biom10030432 · Cited by 197 · see citing works
- Authors
- Suckale, J., & Solimena, M.
- Affiliations
- Paul Langerhans Institute Dresden (DE)
- Max Planck Institute of Molecular Cell Biology and Genetics (DE)
- Corresponding author
- Solimena, Michele
- ORCID
- Solimena, Michele
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2010-10
- Volume
- 21
- Issue
- 10
- Pages
- 599-609
- ISSN
- 1043-2760 (ISSN-L)
- OpenAlex
- W2082432928
- Cited by
- 201
- References
- 4
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 11 · 2023: 14 · 2022: 16 · 2021: 17 · 2020: 19 · 2019: 8 · 2018: 9 · 2017: 14 · 2016: 17 · 2015: 10 · 2014: 6 · 2013: 19 · 2012: 12
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Site cant be reached (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Bundesministerium für Bildung und Forschung
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- Rab3A, Rab27a, PTPRN, PTPRN2, beta-cell proliferation, ATP, GABA, C-peptide, amylin, glucagon secretion, pancreatic beta cells
- MeSH terms
- Insulin Secretion, Adenosine Triphosphate, Animals, Chromogranins, Humans, Insulin, Signal Transduction, Monomeric GTP-Binding Proteins, Secretory Vesicles
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