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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

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.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...

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Multiple signals regulate phospholipase CBeta3 in human myometrial cells.

Miao Zhong1, Dilyara A Murtazina, Jennifer Phillips

  • 1Department of Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80523, USA.

Biology of Reproduction
|March 7, 2008
PubMed
Summary

Phospholipase CB3 (PLCB3) phosphorylation integrates myometrial signaling. cAMP/PRKA pathways negatively crosstalk, while oxytocin/PRKC pathways form a negative feedback loop, regulating myometrial cell function.

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Area of Science:

  • Cellular signaling
  • Molecular biology
  • Reproductive biology

Background:

  • Phospholipase CB3 (PLCB3) serine(1105) is a key substrate in myometrial signaling pathways.
  • Understanding PLCB3 regulation is crucial for myometrial function.

Purpose of the Study:

  • To investigate the regulation of PLCB3-S(1105) phosphorylation in human myometrial cells.
  • To elucidate the crosstalk between different signaling pathways converging on PLCB3.

Main Methods:

  • Utilized immortalized and primary human myometrial cells.
  • Employed pharmacological inhibitors for protein kinases (PRKA, PRKC) and phosphatases (PP1, PP2A, PP2B).
  • Investigated effects of signaling molecules like oxytocin, relaxin, CALCA, and cAMP analogs; assessed intracellular calcium and phosphatidylinositol turnover; used RNA interference for PLCB3 knockdown.

Main Results:

  • CPT-cAMP and CALCA transiently increased PLCB3-S(1105) phosphorylation (P-S(1105)).
  • Oxytocin, prostaglandin F2alpha, and ATP also increased P-S(1105), with oxytocin effects modulated by PRKC inhibitors and phorbol esters.
  • Negative crosstalk from cAMP/PRKA and a PRKC-mediated negative feedback loop in the oxytocin pathway were identified, involving distinct phosphatases for dephosphorylation.

Conclusions:

  • PLCB3 acts as an integration point for diverse signaling pathways in the myometrium.
  • Negative crosstalk and feedback loops involving cAMP/PRKA and oxytocin/PRKC pathways modulate PLCB3 activity.
  • Differential phosphatase involvement in dephosphorylation suggests complex regulation of PLCB3 phosphorylation status.