Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3‐dependent Ca2+ release in vivo

Hennigs, Jan K.; Burhenne, Nicole; Stähler, Frauke; Winnig, Marcel; Walter, Bettina; Meyerhof, Wolfgang; Schmale, Hartwig

doi:10.1111/j.1471-4159.2008.05563.x

Cited by 24 publications

(32 citation statements)

References 54 publications

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“…Neurocalcin has been implicated in the trafficking of neurotransmitter receptors (Coussen and Mulle 2006) and regulates guanylate cyclase activity in the retina ) and olfactory epithelium Duda and Sharma 2008). Other cell signaling regulators have been shown to affect the signaling pathways in type II taste cells (Hennigs et al 2008), so given the high expression levels of neurocalcin in type II cells, it is interesting to speculate that neurocalcin may exert similar effects on the cyclic nucleotide transduction pathways in taste cells (Clapp et al 2008;Trubey et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Rebello

Aktas

Medler

2011

J Histochem Cytochem.

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SummaryIt is well established that calcium is a critical signaling molecule in the transduction of taste stimuli within the peripheral taste system. However, little is known about the regulation and termination of these calcium signals in the taste system. The authors used Western blot, immunocytochemical, and RT-PCR analyses to evaluate the expression of multiple calcium binding proteins in mouse circumvallate taste papillae, including parvalbumin, calbindin D28k, calretinin, neurocalcin, NCS-1 (or frequenin), and CaBP. They found that all of the calcium binding proteins they tested were expressed in mouse circumvallate taste cells with the exception of NCS-1. The authors correlated the expression patterns of these calcium binding proteins with a marker for type II cells and found that neurocalcin was expressed in 80% of type II cells, whereas parvalbumin was found in less than 10% of the type II cells. Calretinin, calbindin, and CaBP were expressed in about half of the type II cells. These data reveal that multiple calcium binding proteins are highly expressed in taste cells and have distinct expression patterns that likely reflect their different roles within taste receptor cells. (J Histochem Cytochem 59:530-539, 2011)

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Section: Discussionmentioning

confidence: 99%

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Rebello

Aktas

Medler

2011

J Histochem Cytochem.

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“…Calcineurin (Cn) was shown to associate with the L-type Ca 2+ channel, which is the major mediator of Ca 2+ influx from the sarcoplasmic reticulum by activating RyR 2 in cardiac myocytes [31]. The binding of CIB1 to αIIbβ3 is identified to inhibit phospholipase C (PLC)/IP 3 signaling [1, 2, 4]. Of note, CIB1 is also reported to inhibit the IP 3 R-Ca 2+ release channel [32].…”

Section: Cib1 and Ca2+ Signalingmentioning

confidence: 99%

“…In general, intracellular Ca 2+ signals result either from its release from the important intracellular stores (such as endoplasmic reticulum (ER) and endo-lysosome), or by activation of Ca 2+ -conducting channels at the plasma membrane, including voltage-dependent Ca 2+ channels (VDCCs), Na + /Ca 2+ exchanger (NCX), plasma membrane calcium-transporting ATPases (PMCAs), cyclic nucleotide-gated ion channels (CNGCs), α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) and N-methyl-D-aspartate receptor (NMDAR) etc [4, 25-29]. Release of intracellular Ca 2+ from ER store through IP 3 R and/or ryanodine receptors (RyR) [25].…”

Section: Cib1 and Ca2+ Signalingmentioning

confidence: 99%

“…Studies suggested that Mg 2+ -CIB1 and Ca 2+ -CIB1 exhibit a more ordered 4-EF-hand structure with smaller hydrodynamic radius than a highly flexible molten globule-like CIB1 (not bound to any metals)[6, 8]. A consensus sequence 5’-MGXXXS/T-3’ at the CIB1 N terminus appears to be crucial for its myristoylation modification and plasma membrane localization [4, 7, 13, 14]. The myristoylation at the CIB1 N terminus might interfere with CIB1 cellular function [13, 15-17].…”

Section: Introductionmentioning

confidence: 99%

“…Calcium and integrin-binding protein 1 (CIB1, also known as calmyrin and KIP) is a 22 kD protein, identified originally as a binding partner of platelet integrin cytoplasmic domain alpha-IIb/beta3(αIIbβ3) [1], and later found to regulate αIIbβ3 activation [2, 3] and down regulate inositol 1, 4,5-trisphosphate receptor (IP 3 R)-dependent calcium (Ca 2+ ) release [4]. As a calcium-binding protein, the structural properties of CIB1 are most closely related to calcineurin B (CnB) (57% sequence similarity to CIB1) and calmodulin (CaM) (56% similarity to CIB1) [1, 5].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The Emerging Roles of CIB1 in Cancer

Wang

Peng

Zhang

et al. 2017

Cell Physiol Biochem

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Calcium and integrin-binding protein 1 (CIB1) is an EF-hand calcium binding protein, which is involved in many cellular processes, including calcium signaling, cell survival and proliferation, cell migration, cell adhesion and apoptosis. A number of studies have found that CIB1 is ubiquitously expressed and is related to various human diseases, such as cancer, Alzheimer’s disease (AD), cardiac hypertrophy and male infertility. The mechanism of CIB1 in human diseases is still not clear, although multiple functions of CIB1 are modulated by interacting with numerous interacting partners. As a calcium binding protein, the roles of CIB1 in calcium signaling by binding calcium or modulating some key modulators, such as calcineurin, integrin, inositol 1,4,5-trisphosphate receptor (IP₃R) and taste 1 receptor member 2 (TAS1R2). The tumor promoting mechanisms of CIB1 have been described in different aspects, including promoting tumor cell cycle and proliferation, inhibiting tumor cell apoptosis, and mediating tumor cell migration and angiogenesis. In addition, multiple functions of CIB1, such as neural development, taste or gustation functions, and virus infection are also elucidated. These recent advances have significantly expanded our understanding of the knowledge of CIB1 and highlighted the potential mechanisms of CIB1 in tumor progression.

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The P2-receptor-mediated Ca2+ signalosome of the human pulmonary endothelium - implications for pulmonary arterial hypertension

Hennigs

Lüneburg

Stage

et al. 2019

Purinergic Signalling

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Dysfunction of the pulmonary endothelium is associated with most lung diseases. Extracellular nucleotides modulate a plethora of endothelial functions in the lung such as vessel integrity, vasodilatation, inflammatory, and thrombotic responses as well as survival and DNA repair, mostly via Ca 2+ signaling pathways. However, a comprehensive analysis of the molecular components of the underlying P2 receptor-mediated Ca 2+ signaling pathways in the lung has not been conducted so far. Therefore, our aim was to identify the principal P2 receptor Ca 2+ signalosome in the human pulmonary endothelium and investigate potential dysregulation in pulmonary vascular disease. Comparative transcriptomics and quantitative immunohistochemistry were performed on publicly available RNA sequencing and protein datasets to identify the specific expression profile of the P2-receptor Ca 2+ signalosome in the healthy human pulmonary endothelium and endothelial cells (EC) dysfunctional due to loss of or defective bone morphogenetic protein receptor (BMPR2). Functional expression of signalosome components was tested by single cell Ca 2+ imaging. Comparative transcriptome analysis of 11 endothelial cell subtypes revealed a specific P2 receptor Ca 2+ signalosome signature for the pulmonary endothelium. Pulmonary endothelial expression of the most abundantly expressed Ca 2+ toolkit genes CALM1, CALM2, VDAC1, and GNAS was confirmed by immunohistochemistry (IHC). P2RX1, P2RX4, P2RY6, and P2YR11 showed strong lung endothelial staining by IHC, P2X5, and P2Y1 were found to a much lesser extent. Very weak or no signals were detected for all other P2 receptors. Stimulation of human pulmonary artery (HPA) EC by purine nucleotides ATP, ADP, and AMP led to robust intracellular Ca 2+ signals mediated through both P2X and P2Y receptors. Pyrimidine UTP and UDP-mediated Ca 2+ signals were generated almost exclusively by activation of P2Y receptors. HPAEC made dysfunctional by siRNA-mediated BMPR2 depletion showed downregulation of 18 and upregulation of 19 P2 receptor Ca 2+ signalosome genes including PLCD4, which was found to be upregulated in iPSC-EC from BMPR2-mutant patients with pulmonary arterial hypertension. In conclusion, the human pulmonary endothelium expresses a distinct functional subset of the P2 receptor Ca 2+ signalosome. Composition of the P2 receptor Ca 2+ toolkit in the pulmonary endothelium is susceptible to genetic disturbances likely contributing to an unfavorable pulmonary disease phenotype found in pulmonary arterial hypertension.

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Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP₃‐dependent Ca²⁺ release in vivo

Cited by 24 publications

References 54 publications

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

The Emerging Roles of CIB1 in Cancer

The P2-receptor-mediated Ca2+ signalosome of the human pulmonary endothelium - implications for pulmonary arterial hypertension

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