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Related Concept Videos

Adrenergic Receptors: ɑ Subtype01:31

Adrenergic Receptors: ɑ Subtype

Adrenoceptors are classified into α and ꞵ classes based on their potencies to catecholamine agonists. α-adrenoceptors show the following order of catecholamine potency:
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase C—inositol-1,4,5-trisphosphate...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Adrenergic Receptors: β Subtype01:26

Adrenergic Receptors: β Subtype

β-adrenoceptors have varied sensitivities towards adrenaline, noradrenaline, and isoprenaline. The order of agonist potency is as follows:
Isoprenaline > Adrenaline > Noradrenaline
Neurotransmitter binding to these receptors causes activation of adenylyl cyclase resulting in increased concentrations of cAMP and modulation of calcium ion channels within the cell. They are further classified into β1, β2, and β3 subtypes.
β1-adrenoceptors: β1-adrenoceptors have equal affinities for...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
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...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

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 cells.
Two...

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Related Experiment Video

Updated: Jul 7, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
10:31

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

Published on: September 26, 2025

Liprin alpha1 interacts with PP2A B56gamma.

Jason D Arroyo1, Grace M Lee, William C Hahn

  • 1Department of Medical Oncology, Dana-Farber Cancer Institute, 44 Binney Street, Dana 1538, Boston, Massachusetts 02115, USA.

Cell Cycle (Georgetown, Tex.)
|February 1, 2008
PubMed
Summary
This summary is machine-generated.

Protein phosphatase 2A (PP2A) B56gamma complexes interact with liprin alpha1, a novel binding partner. This interaction reveals a new role for PP2A B56gamma beyond its phosphatase activity, impacting cell morphology.

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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

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Last Updated: Jul 7, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
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A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

Published on: September 26, 2025

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein phosphatase 2A (PP2A) is a key serine-threonine phosphatase family involved in regulating numerous cellular processes.
  • Inhibition of PP2A contributes to human cell transformation, and specific subunits like B56gamma are crucial for its function.
  • Depletion of PP2A B56gamma complexes in immortalized human cells induces in vitro cell transformation.

Purpose of the Study:

  • To identify novel binding partners of the PP2A B56gamma regulatory subunit.
  • To investigate the functional significance of PP2A B56gamma interacting proteins.
  • To explore potential PP2A B56gamma functions independent of its phosphatase activity.

Main Methods:

  • Tandem affinity purification coupled with mass spectrometry was employed to identify proteins interacting with PP2A B56gamma.
  • RNA interference (RNAi) was used to suppress liprin alpha1 expression.
  • Cell morphology and transformation assays were performed.

Main Results:

  • Liprin alpha1 was identified as a novel protein interacting with PP2A B56gamma.
  • B56gamma-liprin alpha1 complexes were found to be distinct from PP2A complexes containing B56gamma.
  • While liprin alpha1 did not directly cause cell transformation, its suppression via RNAi led to altered cell morphology.

Conclusions:

  • PP2A B56gamma interacts with liprin alpha1, forming distinct complexes.
  • Liprin alpha1's role in altering cell morphology suggests a novel function for PP2A B56gamma independent of its phosphatase activity.
  • These findings open new avenues for understanding PP2A regulation and its role in cell biology.