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Nanoscale organization of CaV2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation.


ABSTRACT: The distance between CaV2.1 voltage-gated Ca2+ channels and the Ca2+ sensor responsible for vesicle release at presynaptic terminals is critical for determining synaptic strength. Yet, the molecular mechanisms responsible for a loose coupling configuration of CaV2.1 in certain synapses or developmental periods and a tight one in others remain unknown. Here, we examine the nanoscale organization of two CaV2.1 splice isoforms (CaV2.1[EFa] and CaV2.1[EFb]) at presynaptic terminals by superresolution structured illumination microscopy. We find that CaV2.1[EFa] is more tightly co-localized with presynaptic markers than CaV2.1[EFb], suggesting that alternative splicing plays a crucial role in the synaptic organization of CaV2.1 channels.

SUBMITTER: Cingolani LA 

PROVIDER: S-EPMC10695435 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature

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Nanoscale organization of Ca<sub>V</sub>2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation.

Cingolani Lorenzo A LA   Thalhammer Agnes A   Jaudon Fanny F   Muià Jessica J   Baj Gabriele G  

Biological chemistry 20230904 10


The distance between Ca<sub>V</sub>2.1 voltage-gated Ca<sup>2+</sup> channels and the Ca<sup>2+</sup> sensor responsible for vesicle release at presynaptic terminals is critical for determining synaptic strength. Yet, the molecular mechanisms responsible for a loose coupling configuration of Ca<sub>V</sub>2.1 in certain synapses or developmental periods and a tight one in others remain unknown. Here, we examine the nanoscale organization of two Ca<sub>V</sub>2.1 splice isoforms (Ca<sub>V</sub>2.  ...[more]

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