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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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...
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IP3/DAG Signaling Pathway01:11

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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...
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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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Adrenergic Receptors: β Subtype01:26

Adrenergic Receptors: β Subtype

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β-adrenoceptors have varied sensitivities towards adrenaline, noradrenaline, and isoprenaline. The order of agonist potency is as follows:
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What are Second Messengers?01:12

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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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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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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Related Experiment Video

Updated: Mar 29, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

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Differential interaction of β2e with phosphoinositides: A comparative study between β2e and MARCKS.

Dong-Il Kim1, Byung-Chang Suh1

  • 1a Department of Brain and Cognitive Sciences, DGIST , Daegu , Korea.

Channels (Austin, Tex.)
|December 10, 2015
PubMed
Summary

The CaV β2e subunit and MARCKS protein bind cell membranes electrostatically but are regulated differently. Poly-phosphoinositide levels control CaV β2e localization, while PKC activation affects MARCKS.

Keywords:
electrostatic interactionmyristoylated alanine-rich C kinase substrate (MARCKS)phosphatidylinositol 4,5-bisphosphate (PIP2)protein kinase C (PKC)voltage-gated calcium channelβ2e subunit

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

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Area of Science:

  • Cellular Biology
  • Molecular Neuroscience
  • Biophysics

Background:

  • Voltage-gated calcium (CaV) channels regulate Ca(2+) influx in excitable cells.
  • CaV β subunits are crucial auxiliary proteins influencing CaV channel expression and function.
  • Subcellular localization of CaV β subunits dictates channel biophysical properties.

Purpose of the Study:

  • To investigate the membrane interaction properties of the CaV β2e subunit.
  • To compare the membrane binding and regulation of CaV β2e with myristoylated alanine-rich C kinase substrate (MARCKS).
  • To elucidate the differential regulation of these proteins by membrane phospholipids and enzymatic activity.

Main Methods:

  • Charge neutralization of the inner plasma membrane leaflet.
  • Transient depletion of poly-phosphoinositides (poly-PIs) using translocatable pseudojanin (PJ) systems.
  • Protein kinase C (PKC) activation assays.
  • Confocal microscopy for subcellular localization studies.

Main Results:

  • Both β2e and MARCKS translocated to the cytosol upon charge neutralization of the inner membrane leaflet.
  • Poly-PI depletion caused β2e translocation but not MARCKS translocation.
  • PKC activation induced MARCKS translocation, but not β2e translocation.
  • Poly-PI depletion slowed MARCKS recovery to the plasma membrane after activation.

Conclusions:

  • CaV β2e and MARCKS bind to the plasma membrane via electrostatic interactions.
  • These proteins exhibit distinct regulatory mechanisms controlling their membrane association.
  • CaV β2e localization is primarily regulated by poly-PI levels, whereas MARCKS is regulated by PKC activation and PI availability.