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Related Concept Videos

Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

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Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
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Amplifying Signals via Enzymatic Cascade01:22

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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...
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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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Amplifying Signals via Second Messengers01:15

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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...
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Diversity in Cell Signaling Responses01:22

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The physiological function of a cell and cellular communication are outcomes of a range of extrinsic signals, intracellular signaling pathways, and cellular responses. No two cell types express the same repertoire of signaling components. Receptors are highly selective for their cognate ligands, but once activated, they can alter multiple cellular processes such as DNA transcription, protein synthesis, and metabolic activity. 
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Related Experiment Video

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Detection of Signaling Effector-Complexes Downstream of BMP4 Using in situ PLA, a Proximity Ligation Assay
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PLCε mediated sustained signaling pathways.

Stephanie S Dusaban1, Joan Heller Brown2

  • 1Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093, USA; Biomedical Sciences Graduate Program, University of California, San Diego, La Jolla, CA 92093, USA.

Advances in Biological Regulation
|December 3, 2014
PubMed
Summary

Phospholipase C-ε (PLCε) integrates G-protein coupled receptor signals, acting as both a catalyst and a Rap1 exchange factor. Its unique feedback mechanism contributes to sustained signaling, implicating it in diseases like cancer and ischemia.

Keywords:
Diacylglycerol (DAG)G-protein coupled receptors (GPCRs)GolgiInositol 1,4,5-trisphosphate (IP3)Phosphatidylinositol4,5-bisphosphate (PIP2)Phospholipase C-ε (PLCε)Protein kinase D(PKD)Rap1RasRhoA

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Area of Science:

  • Biochemistry
  • Cellular Signaling
  • Molecular Biology

Background:

  • Phospholipase C-ε (PLCε) is a key enzyme integrating G-protein coupled receptor (GPCR) signaling pathways.
  • Unlike other phospholipases, PLCε possesses both catalytic activity for phosphoinositide hydrolysis and guanine nucleotide exchange factor activity for the small G-protein Rap1.
  • Its unique regulatory mechanisms are crucial for understanding cellular responses and disease pathogenesis.

Purpose of the Study:

  • To review the multifaceted regulation of Phospholipase C-ε (PLCε).
  • To elucidate the molecular mechanisms underlying sustained signaling mediated by PLCε.
  • To discuss the involvement of PLCε in diverse pathological conditions.

Main Methods:

  • Literature review focusing on PLCε function and regulation.
  • Analysis of signaling pathways involving GPCRs, RhoA, and Rap1.
  • Examination of PLCε's role in disease models.

Main Results:

  • PLCε is selectively activated by GPCR agonists coupled to RhoA, which directly bind and modulate its activity.
  • Rap1 binding to the PLCε RA2 domain creates a feedback loop, sustaining cellular signaling.
  • PLCε's dual catalytic and exchange factor functions are central to its biological roles.

Conclusions:

  • PLCε plays a critical role in integrating GPCR-mediated signals to downstream kinases.
  • The enzyme's ability to generate sustained signals, influenced by inflammatory GPCR ligands, links it to diseases such as cancer and ischemia/reperfusion injury.
  • Understanding PLCε regulation and mechanisms is vital for therapeutic strategies targeting related diseases.