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  Molecular and functional architecture of striatal dopamine release sites

Banerjee, A., Imig, C., Balakrishnan, K., Kershberg, L., Lipstein, N., Uronen, R.-K., et al. (2022). Molecular and functional architecture of striatal dopamine release sites. Neuron, 110(2), 248-265.e9. doi:10.1016/j.neuron.2021.10.028.

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Banerjee, A., Author
Imig, C.1, Author              
Balakrishnan, K., Author
Kershberg, L., Author
Lipstein, N.1, Author              
Uronen, R.-K.1, Author              
Wang, J., Author
Cai, X., Author
Benseler, F.1, Author              
Rhee, J. S.1, Author              
Cooper, B. H.1, Author              
Liu, C., Author
Wojcik, S. M.1, Author              
Brose, N.1, Author              
Kaeser, P. S., Author
Affiliations:
1Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173659              

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Free keywords: Liprin-α; Munc13; RIM-BP; RIM1α; basal ganglia; dopamine; neuromodulation; secretion; striatum
 Abstract: Despite the importance of dopamine for striatal circuit function, mechanistic understanding of dopamine transmission remains incomplete. We recently showed that dopamine secretion relies on the presynaptic scaffolding protein RIM, indicating that it occurs at active zone-like sites similar to classical synaptic vesicle exocytosis. Here, we establish using a systematic gene knockout approach that Munc13 and Liprin-α, active zone proteins for vesicle priming and release site organization, are important for dopamine secretion. Furthermore, RIM zinc finger and C2B domains, which bind to Munc13 and Liprin-α, respectively, are needed to restore dopamine release after RIM ablation. In contrast, and different from typical synapses, the active zone scaffolds RIM-BP and ELKS, and RIM domains that bind to them, are expendable. Hence, dopamine release necessitates priming and release site scaffolding by RIM, Munc13, and Liprin-α, but other active zone proteins are dispensable. Our work establishes that efficient release site architecture mediates fast dopamine exocytosis.

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Language(s): eng - English
 Dates: 2021-11-112022-01-19
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.neuron.2021.10.028
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Title: Neuron
Source Genre: Journal
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Pages: - Volume / Issue: 110 (2) Sequence Number: - Start / End Page: 248 - 265.e9 Identifier: ISSN: 08966273