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Interaction with a kinesin-2 tail propels choline acetyltransferase flow towards synapse. [Drosophila facility]

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TitleInteraction with a kinesin-2 tail propels choline acetyltransferase flow towards synapse. [Drosophila facility]
Publication TypeJournal Article
Year of Publication2012
AuthorsSadananda A, Hamid R, Doodhi H, Ghosal D, Girotra M, Jana SChandra, Ray K
JournalTraffic
Volume13
Issue7
Pagination979-91
Date Published2012 Jul
ISSN1600-0854
KeywordsAnimals, Animals, Genetically Modified, Axonal Transport, Carrier Proteins, Choline O-Acetyltransferase, Cholinergic Neurons, Drosophila, Drosophila Proteins, Fluorescence Recovery After Photobleaching, Kinesin, Larva, Microtubule-Associated Proteins, Protein Interaction Domains and Motifs, Synapses
Abstract

Bulk flow constitutes a substantial part of the slow transport of soluble proteins in axons. Though the underlying mechanism is unclear, evidences indicate that intermittent, kinesin-based movement of large protein-aggregates aids this process. Choline acetyltransferase (ChAT), a soluble enzyme catalyzing acetylcholine synthesis, propagates toward the synapse at an intermediate, slow rate. The presynaptic enrichment of ChAT requires heterotrimeric kinesin-2, comprising KLP64D, KLP68D and DmKAP, in Drosophila. Here, we show that the bulk flow of a recombinant Green Fluorescent Protein-tagged ChAT (GFP::ChAT), in Drosophila axons, lacks particulate features. It occurs for a brief period during the larval stages. In addition, both the endogenous ChAT and GFP::ChAT directly bind to the KLP64D tail, which is essential for the GFP::ChAT entry and anterograde flow in axon. These evidences suggest that a direct interaction with motor proteins could regulate the bulk flow of soluble proteins, and thus establish their asymmetric distribution.

DOI10.1111/j.1600-0854.2012.01361.x
Alternate JournalTraffic
PubMed ID22486887
PubMed Central IDPMC3374014
Grant ListR03 TW005784-01 / TW / FIC NIH HHS / United States
1 R03 TW05784 / TW / FIC NIH HHS / United States