Calmodulin and S100A1 Protein Interact with N Terminus of TRPM3 Channel

Holakovska, Blanka; Grycová, Lenka; Jirku, Michaela; Šulc, Miroslav; Bumba, Ladislav; Teisinger, Jan

doi:10.1074/jbc.m112.350686

Cited by 44 publications

(79 citation statements)

References 35 publications

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“…TRP channel opening frequency is reportedly controlled by PIP2 [59][60][61][62] and inhibited by calmodulin. 59,[63][64][65] Studying these proteins in context of growth factor-stimulated calcium influx and EMT may be of interest. However, regulation by PIP2 or calmodulin does not explain why microtubule targeting agents inhibit high frequency calcium influxes following HGF stimulation.…”

Section: Molecular Control Of Calcium Influxes Upon Induction Of Epitmentioning

confidence: 99%

Control of cell mechanics by RhoA and calcium fluxes during epithelial scattering

2016

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Epithelial tissues use adherens junctions to maintain tight interactions and coordinate cellular activities. Adherens junctions are remodeled during epithelial morphogenesis, including instances of epithelialmesenchymal transition, or EMT, wherein individual cells detach from the tissue and migrate as individual cells. EMT has been recapitulated by growth factor induction of epithelial scattering in cell culture. In culture systems, cells undergo a highly reproducible series of cell morphology changes, most notably cell spreading followed by cellular compaction and cell migration. These morphology changes are accompanied by striking actin rearrangements. The current evidence suggests that global changes in actomyosin-based cellular contractility, first a loss of contractility during spreading and its activation during cell compaction, are the main drivers of epithelial scattering. In this review, we focus on how spreading and contractility might be controlled during epithelial scattering. While we propose a central role for RhoA, which is well known to control cellular contractility in multiple systems and whose role in epithelial scattering is well accepted, we suggest potential roles for additional cellular systems whose role in epithelial cell biology has been less well documented. In particular, we propose critical roles for vesicle recycling, calcium channels, and calcium-dependent kinases.

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Section: Molecular Control Of Calcium Influxes Upon Induction Of Epitmentioning

confidence: 99%

Control of cell mechanics by RhoA and calcium fluxes during epithelial scattering

2016

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“…1A) and all of them have a homotetrameric structure [11][12][13][14]. Intracellularly located N-and C-tails are responsible for the regulation of TRP channels, which carry binding sites for signal ligands such as the intracellular calcium binding protein calmodulin [15,16] or plasma membrane lipid phosphatidylinositol-4,5-bisphosphate (PIP2) [17][18][19][20].…”

Section: Contents Lists Available At Sciencedirectmentioning

confidence: 99%

PIP2 and PIP3 interact with N-terminus region of TRPM4 channel

Boušová

Jirku

Bumba

et al. 2015

Biophysical Chemistry

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“…TRPM3 contains the TRP domain, a highly conserved motif, located on the C-terminal side of the sixth transmembrane domain. In addition, calmodulin-binding sites have been detected within the N-terminal cytosolic domain of TRPM3 (Halokovska et al 2012). The modular structure of TRPM3 is depicted in Fig.…”

Section: Introductionmentioning

confidence: 99%

Signal transduction via TRPM3 channels in pancreatic β-cells

Thiel

Muller

Rößler

2013

Journal of Molecular Endocrinology

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Transient receptor potential melastatin 3 (TRPM3) channels are non-selective cation channels that are expressed in insulinoma cells and pancreatic b-cells. Stimulation of TRPM3 with the neurosteroid pregnenolone sulfate induces an intracellular signaling cascade, involving a rise in intracellular Ca 2C concentration, activation of the protein kinases Raf and ERK, and a change in the gene expression pattern of the cells. In particular, biosynthesis of insulin is altered following activation of TRPM3 by pregnenolone sulfate. Moreover, a direct effect of TRPM3 stimulation on insulin secretion has been reported. The fact that stimulation of TRPM3 induces a signaling cascade that is very similar to the signaling cascade induced by glucose in b-cells suggests that TRPM3 may influence main functions of pancreatic b-cells. The view that TRPM3 represents an ionotropic steroid receptor of pancreatic b-cells linking insulin release with steroid hormone signaling is discussed.

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Calmodulin and S100A1 Protein Interact with N Terminus of TRPM3 Channel

Cited by 44 publications

References 35 publications

Control of cell mechanics by RhoA and calcium fluxes during epithelial scattering

Control of cell mechanics by RhoA and calcium fluxes during epithelial scattering

PIP2 and PIP3 interact with N-terminus region of TRPM4 channel

Signal transduction via TRPM3 channels in pancreatic β-cells

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