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Related Concept Videos

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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Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: Sep 12, 2025

Live Imaging of Synaptic Vesicle Recycling in the Neuromuscular Junction of Dissected Larval Zebrafish
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Published on: February 7, 2025

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Distinct Roles of CaMKII in Synaptic Vesicle Dynamics at Zebrafish Retinal Rod Bipolar Ribbon Synapses.

Johane M Boff, Nirujan Rameshkumar, Moumita Khamrai

    Biorxiv : the Preprint Server for Biology
    |August 6, 2025
    PubMed
    Summary

    Calcium/calmodulin-dependent protein kinase II (CaMKII) optimally regulates neurotransmitter release at presynaptic terminals. Both CaMKII inhibition and activation impair vesicle fusion, while CaMKII activity is crucial for synaptic vesicle replenishment.

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    Area of Science:

    • Neuroscience
    • Cell Biology
    • Synaptic Transmission

    Background:

    • Calcium (Ca²⁺) is a key regulator of neurotransmitter release (NTR).
    • Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) is present at presynaptic terminals and may modulate NTR.
    • Conflicting data exist on CaMKII's role in NTR at rod bipolar cell (RBC) ribbon synapses.

    Purpose of the Study:

    • To investigate the precise role of CaMKII in regulating NTR at zebrafish RBC ribbon synapses.
    • To determine how manipulating CaMKII activity affects Ca²⁺ signaling, exocytosis, and synaptic vesicle dynamics.

    Main Methods:

    • Acutely manipulated CaMKII activity in zebrafish RBC presynaptic terminals using inhibitory peptides or constitutively active CaMKII.
    • Employed a combination of imaging and electrophysiological approaches.
    • Measured Ca²⁺ channel activity, exocytosis via capacitance measurements, and synaptic vesicle replenishment.

    Main Results:

    • CaMKII manipulation did not affect presynaptic Ca²⁺ channel activity.
    • Inhibition or activation of CaMKII reduced exocytosis.
    • CaMKII inhibition impaired synaptic vesicle replenishment, while CaMKII activation did not.

    Conclusions:

    • CaMKII activity is optimally tuned for neurotransmitter release at RBC ribbon synapses.
    • CaMKII plays distinct roles in regulating exocytosis and synaptic vesicle replenishment.
    • Different synaptic vesicle pools exhibit differential dependence on CaMKII activity levels.