突触前末端CaV2.1剪接异构体的纳米级组织：对突触小泡释放和突触促进的意义。

IF 2.9 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biological Chemistry Pub Date : 2023-09-04 Print Date: 2023-09-26 DOI:10.1515/hsz-2023-0235

Lorenzo A Cingolani, Agnes Thalhammer, Fanny Jaudon, Jessica Muià, Gabriele Baj

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引用次数: 0

摘要

CaV2.1电压门控Ca2+通道和负责突触前末端囊泡释放的Ca2+传感器之间的距离对于确定突触强度至关重要。然而，导致CaV2.1在某些突触或发育期出现松散耦合配置，而在其他突触或发育时期出现紧密耦合配置的分子机制仍然未知。在这里，我们通过超分辨率结构照明显微镜检查了两种CaV2.1剪接异构体（CaV2.1[EFa]和CaV2.1[EFb]）在突触前末端的纳米级组织。我们发现，与CaV2.1[EFb]相比，CaV2.1[EFa]与突触前标记物更紧密地共定位，这表明选择性剪接在CaV2.1通道的突触组织中起着至关重要的作用。

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Nanoscale organization of Ca_V2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation.

The distance between Ca_V2.1 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 Ca_V2.1 in certain synapses or developmental periods and a tight one in others remain unknown. Here, we examine the nanoscale organization of two Ca_V2.1 splice isoforms (Ca_V2.1[EFa] and Ca_V2.1[EFb]) at presynaptic terminals by superresolution structured illumination microscopy. We find that Ca_V2.1[EFa] is more tightly co-localized with presynaptic markers than Ca_V2.1[EFb], suggesting that alternative splicing plays a crucial role in the synaptic organization of Ca_V2.1 channels.

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来源期刊

Biological Chemistry 生物-生化与分子生物学

CiteScore

7.20

自引率

0.00%

发文量

审稿时长

4-8 weeks

期刊介绍： Biological Chemistry keeps you up-to-date with all new developments in the molecular life sciences. In addition to original research reports, authoritative reviews written by leading researchers in the field keep you informed about the latest advances in the molecular life sciences. Rapid, yet rigorous reviewing ensures fast access to recent research results of exceptional significance in the biological sciences. Papers are published in a "Just Accepted" format within approx.72 hours of acceptance.