Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells

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Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells. / Lønsmann, Ida; Bak, Lasse K.

In: Cellular Signalling, Vol. 72, 109635, 08.2020.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Lønsmann, I & Bak, LK 2020, 'Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells', Cellular Signalling, vol. 72, 109635. https://doi.org/10.1016/j.cellsig.2020.109635

APA

Lønsmann, I., & Bak, L. K. (2020). Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells. Cellular Signalling, 72, [109635]. https://doi.org/10.1016/j.cellsig.2020.109635

Vancouver

Lønsmann I, Bak LK. Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells. Cellular Signalling. 2020 Aug;72. 109635. https://doi.org/10.1016/j.cellsig.2020.109635

Author

Lønsmann, Ida ; Bak, Lasse K. / Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells. In: Cellular Signalling. 2020 ; Vol. 72.

Bibtex

@article{c7ba5482f5124f81a706147f1f566f1d,
title = "Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells",
abstract = "Glucose-stimulated insulin secretion from pancreatic β cells is mediated by Ca2+ influx and amplified by stimulation of GLP-1-receptors through cAMP-based signaling pathways. Interestingly, it has been found that glucose-induced Ca2+ signals can induce concurrent adenylyl cyclase isoform 8 (AC8)-mediated cAMP signals and, conversely, that GLP-1-receptor-mediated cAMP signals are able to induce Ca2+ signals. In this review, we explore the signaling complexes revolving around AC8 in modulating insulin release, from the initial discovery of the importance of this AC isoform to recent investigations of its interacting molecular partners. We suggest that investigating the structural assembly of the proteins associated with AC8 in β cells might reveal how this particular protein complex could be targeted to modify insulin secretion. Specifically, we suggest that disrupting the protein-protein interaction between A-kinase anchoring protein 79 (AKAP79) and AC8 could lead to disinhibition of AC8 activity and increased insulin secretion. Potentially, AC8 protein interactions could become a future target in type 2 diabetic patients with dysfunction of insulin secretion.",
keywords = "Adenylyl cyclase 8 (AC8), AKAP, Compartmentalization, GLP-1, GSIS, Type 2 diabetes",
author = "Ida L{\o}nsmann and Bak, {Lasse K.}",
year = "2020",
month = aug,
doi = "10.1016/j.cellsig.2020.109635",
language = "English",
volume = "72",
journal = "Cellular Signalling",
issn = "0898-6568",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Potential role of adenylyl cyclase 8 signaling complexes in regulating insulin secretion from pancreatic beta cells

AU - Lønsmann, Ida

AU - Bak, Lasse K.

PY - 2020/8

Y1 - 2020/8

N2 - Glucose-stimulated insulin secretion from pancreatic β cells is mediated by Ca2+ influx and amplified by stimulation of GLP-1-receptors through cAMP-based signaling pathways. Interestingly, it has been found that glucose-induced Ca2+ signals can induce concurrent adenylyl cyclase isoform 8 (AC8)-mediated cAMP signals and, conversely, that GLP-1-receptor-mediated cAMP signals are able to induce Ca2+ signals. In this review, we explore the signaling complexes revolving around AC8 in modulating insulin release, from the initial discovery of the importance of this AC isoform to recent investigations of its interacting molecular partners. We suggest that investigating the structural assembly of the proteins associated with AC8 in β cells might reveal how this particular protein complex could be targeted to modify insulin secretion. Specifically, we suggest that disrupting the protein-protein interaction between A-kinase anchoring protein 79 (AKAP79) and AC8 could lead to disinhibition of AC8 activity and increased insulin secretion. Potentially, AC8 protein interactions could become a future target in type 2 diabetic patients with dysfunction of insulin secretion.

AB - Glucose-stimulated insulin secretion from pancreatic β cells is mediated by Ca2+ influx and amplified by stimulation of GLP-1-receptors through cAMP-based signaling pathways. Interestingly, it has been found that glucose-induced Ca2+ signals can induce concurrent adenylyl cyclase isoform 8 (AC8)-mediated cAMP signals and, conversely, that GLP-1-receptor-mediated cAMP signals are able to induce Ca2+ signals. In this review, we explore the signaling complexes revolving around AC8 in modulating insulin release, from the initial discovery of the importance of this AC isoform to recent investigations of its interacting molecular partners. We suggest that investigating the structural assembly of the proteins associated with AC8 in β cells might reveal how this particular protein complex could be targeted to modify insulin secretion. Specifically, we suggest that disrupting the protein-protein interaction between A-kinase anchoring protein 79 (AKAP79) and AC8 could lead to disinhibition of AC8 activity and increased insulin secretion. Potentially, AC8 protein interactions could become a future target in type 2 diabetic patients with dysfunction of insulin secretion.

KW - Adenylyl cyclase 8 (AC8)

KW - AKAP

KW - Compartmentalization

KW - GLP-1

KW - GSIS

KW - Type 2 diabetes

U2 - 10.1016/j.cellsig.2020.109635

DO - 10.1016/j.cellsig.2020.109635

M3 - Review

C2 - 32283257

AN - SCOPUS:85083286854

VL - 72

JO - Cellular Signalling

JF - Cellular Signalling

SN - 0898-6568

M1 - 109635

ER -

ID: 240329117