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  The Calmodulin Binding Region of the Synaptic Vesicle Protein Mover Is Required for Homomeric Interaction and Presynaptic Targeting

Akula, A. K., Zhang, X., Viotti, J. S., Nestvogel, D. B., Rhee, H. J., Ebrecht, R., et al. (2019). The Calmodulin Binding Region of the Synaptic Vesicle Protein Mover Is Required for Homomeric Interaction and Presynaptic Targeting. EPJ Web of Conferences, 12: 249. doi:10.3389/fnmol.2019.00249.

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 Creators:
Akula, Asha Kiran, Author
Zhang, Xin, Author
Viotti, Julio S., Author
Nestvogel, Dennis Bernd1, Author           
Rhee, Hong Jun1, Author           
Ebrecht, R., Author
Reim, Kerstin1, Author           
Wouters, Fred, Author
Liepold, Thomas2, Author           
Jahn, Olaf2, Author           
Bogeski, Ivan, Author
Dresbach, Thomas, Author
Affiliations:
1Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173659              
2Molecular neuroendocrinology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173662              

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Free keywords: synaptic vesicle, mover, TPRGL, calmodulin, presynaptic
 Abstract: Neurotransmitter release is mediated by an evolutionarily conserved machinery. The
synaptic vesicle (SV) associated protein Mover/TPRGL/SVAP30 does not occur in all
species and all synapses. Little is known about its molecular properties and how it may
interact with the conserved components of the presynaptic machinery. Here, we show by
deletion analysis that regions required for homomeric interaction of Mover are distributed
across the entire molecule, including N-terminal, central and C-terminal regions. The
same regions are also required for the accumulation of Mover in presynaptic terminals of
cultured neurons. Mutating two phosphorylation sites in N-terminal regions did not affect
these properties. In contrast, a point mutation in the predicted Calmodulin (CaM) binding
sequence of Mover abolished both homomeric interaction and presynaptic targeting.
We show that this sequence indeed binds Calmodulin, and that recombinant Mover
increases Calmodulin signaling upon heterologous expression. Our data suggest that
presynaptic accumulation of Mover requires homomeric interaction mediated by regions
distributed across large areas of the protein, and corroborate the hypothesis that Mover
functionally interacts with Calmodulin signaling.

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Language(s): eng - English
 Dates: 2019-11-08
 Publication Status: Published online
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fnmol.2019.00249
 Degree: -

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Title: EPJ Web of Conferences
Source Genre: Journal
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Pages: 19 Volume / Issue: 12 Sequence Number: 249 Start / End Page: - Identifier: ISSN: 2100-014X
CoNE: https://pure.mpg.de/cone/journals/resource/2100-014X