Faculty Collaboration Database

Nanoscale organization of Ca_V2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation. Biol Chem 2023 Sep 26;404(10):931-937

Date

09/02/2023

Pubmed ID

37658578

Pubmed Central ID

PMC10695435

DOI

10.1515/hsz-2023-0235

Scopus ID

2-s2.0-85170055337 (requires institutional sign-in at Scopus site)   3 Citations

Abstract

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.

Author List

Cingolani LA, Thalhammer A, Jaudon F, Muià J, Baj G

Author

Joshua Muia PhD Assistant Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Calcium Channels, N-Type
Presynaptic Terminals
Protein Isoforms
Synapses
Synaptic Vesicles