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Related Concept Videos

G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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Regulation of Sodium and Potassium01:26

Regulation of Sodium and Potassium

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The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily...
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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several...
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Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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Related Experiment Video

Updated: Dec 21, 2025

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

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FMRP differentially regulates BK channels.

Ben Short

    The Journal of General Physiology
    |May 15, 2020
    PubMed
    Summary

    The fragile X syndrome-associated protein FMRP interacts with BK channels, altering their function. This discovery offers new insights into fragile X syndrome-associated protein FMRP and BK channel regulation.

    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Genetics

    Background:

    • Fragile X syndrome is a genetic disorder associated with intellectual disability.
    • The fragile X syndrome-associated protein (FMRP) is crucial for neuronal development.
    • BK channels are large-conductance calcium-activated potassium channels involved in various physiological processes.

    Discussion:

    • This study investigates the novel interaction between FMRP and BK channels.
    • FMRP's modulation of BK channel kinetics suggests a direct role in regulating neuronal excitability.
    • Understanding this interaction may elucidate mechanisms underlying fragile X syndrome pathophysiology.

    Key Insights:

    • FMRP directly interacts with multiple types of BK channels.
    • FMRP differentially modulates the kinetics of various BK channel subtypes.

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    Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
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    Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration
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    Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
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  • This interaction provides a potential molecular link between FMRP dysfunction and neuronal dysfunction in fragile X syndrome.

    • Outlook:

    • Further research is needed to elucidate the precise mechanisms of FMRP-BK channel interaction.
    • Targeting this interaction could offer novel therapeutic strategies for fragile X syndrome.
    • Investigating FMRP's role in other ion channel functions may reveal broader implications for neurodevelopmental disorders.