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Calmodulin-dependent Signaling01:16

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Catenins01:23

Catenins

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Inhibition of Cdk Activity02:34

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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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Regulation of Polycystin-1 Function by Calmodulin Binding.

Nicholas Doerr1, Yidi Wang1, Kevin R Kipp1

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Autosomal Dominant Polycystic Kidney Disease (ADPKD) involves polycystin-1 (PC1) and polycystin-2 (PC2) mutations. PC1

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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Area of Science:

  • Nephrology
  • Molecular Biology
  • Genetics

Background:

  • Autosomal Dominant Polycystic Kidney Disease (ADPKD) is a prevalent genetic disorder characterized by progressive kidney cyst development and declining renal function.
  • ADPKD pathogenesis is linked to mutations in polycystin-1 (PC1) and polycystin-2 (PC2) genes, whose protein products form a complex in primary cilia.
  • The precise roles of polycystins, their regulation, and the function of the PC1/PC2 channel remain incompletely understood.

Purpose of the Study:

  • To investigate the interaction of the PC1 C-terminal tail with calmodulin (CaM) and its impact on PC1/PC2 channel activity and cellular function.
  • To elucidate the role of calcium-dependent CaM binding in regulating PC1 function.

Main Methods:

  • Bioinformatic analysis to identify conserved motifs in the PC1 tail.
  • Site-directed mutagenesis to disrupt the CaM-binding motif in PC1.
  • Assessment of PC2 binding, ciliary localization, G-protein and STAT3 signaling.
  • Measurement of PC1/PC2 calcium channel activity and flow-dependent calcium responses in kidney epithelial cells.
  • Analysis of cellular energy metabolism in cells expressing wild-type and mutant PC1.

Main Results:

  • The PC1 C-terminal tail exhibits homology to myosin heavy chain regulatory domains, containing a conserved calmodulin-binding motif that binds CaM in a calcium-dependent manner.
  • Disruption of the CaM-binding motif did not affect PC2 interaction, ciliary localization, or signaling through G-proteins or STAT3.
  • However, abrogating CaM binding impaired PC1/PC2 calcium channel activity and the flow-induced calcium response in kidney cells.
  • Expression of the CaM-binding mutant PC1 led to disruptions in cellular energy metabolism.

Conclusions:

  • PC1's ability to bind calmodulin in a calcium-dependent manner is crucial for its function as a flow-sensitive calcium channel.
  • This interaction regulates critical PC1 functions, including cellular energy metabolism, suggesting PC1 acts as a calcium sensor via CaM binding.
  • These findings offer new insights into ADPKD pathogenesis and potential therapeutic targets.