The regulation of insulin secretion via phosphoinositide-specific phospholipase Cβ signaling

Hwang, Hyeon-Jeong; Jang, Hyun‐Jun; Cocco, Lucio; Suh, Pann‐Ghill

doi:10.1016/j.jbior.2018.09.011

Cited by 10 publications

(6 citation statements)

References 83 publications

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“…Down regulation of PLC-XD3 from β-cells, INS-1 cell line, resulted in decreased insulin secretion when stimulated with high glucose [393]. It would appear that insulin secretion can be modulated by different PLCs as some GPCRs use PLCβ1 to modulate glucose-stimulated insulin secretion as discussed above [178,179].…”

Section: Plc-xd Familymentioning

confidence: 95%

“…Several GPCRs on the islet cells including arg-vasopressin, 5-hydroxytryptamine and kisspeptin enhance glucose-stimulated insulin release and β-cells prepared from mice lacking islet-expressed PLCβ1 exhibited a marked defect in glucose-stimulated insulin release, leading to glucose intolerance. Furthermore, the conditional knockout mice when maintained on a high fat diet developed an even more severe glucose intolerance [178,179]. Although islets expressed at least three of the four PLCβs isozymes, only conditional knockout of PLCβ1 resulted in defects in enhanced glucose-stimulated insulin secretion.…”

Section: Plcβ1mentioning

confidence: 99%

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Phospholipase C families: Common themes and versatility in physiology and pathology

Katan

Cockcroft

2020

Progress in Lipid Research

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Section: Plc-xd Familymentioning

confidence: 95%

Section: Plcβ1mentioning

confidence: 99%

Phospholipase C families: Common themes and versatility in physiology and pathology

Katan

Cockcroft

2020

Progress in Lipid Research

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“…The presence of multiple PLCs with distinct regulatory links provides differential means of regulation of PLC activity, reflected in great diversity of their biological functions; this is illustrated here by several examples. Among many roles, ubiquitously expressed PLCβ1 enzyme has been implicated in control of neuronal function and the enhancement of glucose-stimulated insulin secretion in pancreatic β-cells downstream of specific GPCRs in these different cell types [36][37][38][39][40]. PLCγ2, highly expressed in hematopoietic cells, has the key role in signalling downstream of ITAM-associated receptors; for example, it controls multiple functions of B cells, and several types of innate immune cells in response to stimulation of the B-cell antigen receptor (BCR) and Fc receptors (FcRs), respectively [41,42].…”

Section: Plc Signalling Plc Families Their Regulation and Biologicalmentioning

confidence: 99%

Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane

Katan

Cockcroft

2020

Essays in Biochemistry

115

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Phosphatidylinositol(4,5) bisphosphate (PI(4,5)P2) has become a major focus in biochemistry, cell biology and physiology owing to its diverse functions at the plasma membrane. As a result, the functions of PI(4,5)P2 can be explored in two separate and distinct roles – as a substrate for phospholipase C (PLC) and phosphoinositide 3-kinase (PI3K) and as a primary messenger, each having unique properties. Thus PI(4,5)P2 makes contributions in both signal transduction and cellular processes including actin cytoskeleton dynamics, membrane dynamics and ion channel regulation. Signalling through plasma membrane G-protein coupled receptors (GPCRs), receptor tyrosine kinases (RTKs) and immune receptors all use PI(4,5)P2 as a substrate to make second messengers. Activation of PI3K generates PI(3,4,5)P3 (phosphatidylinositol(3,4,5)trisphosphate), a lipid that recruits a plethora of proteins with pleckstrin homology (PH) domains to the plasma membrane to regulate multiple aspects of cellular function. In contrast, PLC activation results in the hydrolysis of PI(4,5)P2 to generate the second messengers, diacylglycerol (DAG), an activator of protein kinase C and inositol(1,4,5)trisphosphate (IP3/I(1,4,5)P3) which facilitates an increase in intracellular Ca2+. Decreases in PI(4,5)P2 by PLC also impact on functions that are dependent on the intact lipid and therefore endocytosis, actin dynamics and ion channel regulation are subject to control. Spatial organisation of PI(4,5)P2 in nanodomains at the membrane allows for these multiple processes to occur concurrently.

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“…Since the first evidence of the existence of PLCs in 1953 [77], 13 mammalian PLC isozymes have been identified so far and they are divided into six subfamilies (β, γ, ε, δ, ζ, η). Interestingly, all PLC isozymes show highly conserved domains (X and Y), as well as unique mingled domains (C2 domain, the EF-hand motif, and the pleckstrin homology domain) [78]. The activation and regulation of PLC isozymes differ in their peculiar subtype structure.…”

Section: Plcsmentioning

confidence: 99%

Nuclear Inositides and Inositide-Dependent Signaling Pathways in Myelodysplastic Syndromes

Xian

Obeng

Ratti

et al. 2020

Cells

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Myelodysplastic syndromes (MDS) are a heterogeneous group of hematological malignancies characterized by peripheral blood cytopenia and abnormal myeloproliferation, as well as a variable risk of evolution into acute myeloid leukemia (AML). The nucleus is a highly organized organelle with several distinct domains where nuclear inositides localize to mediate essential cellular events. Nuclear inositides play a critical role in the modulation of erythropoiesis or myelopoiesis. Here, we briefly review the nuclear structure, the localization of inositides and their metabolic enzymes in subnuclear compartments, and the molecular aspects of nuclear inositides in MDS.

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The regulation of insulin secretion via phosphoinositide-specific phospholipase Cβ signaling

Cited by 10 publications

References 83 publications

Phospholipase C families: Common themes and versatility in physiology and pathology

Phospholipase C families: Common themes and versatility in physiology and pathology

Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane

Nuclear Inositides and Inositide-Dependent Signaling Pathways in Myelodysplastic Syndromes

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