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Journal Article

Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter.

MPS-Authors
/persons/resource/persons14947

Chua,  J. J. E.
Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons14918

Butkevich,  E.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15151

Gronborg,  M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14827

Behrmann,  E.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15266

Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://www.pnas.org/content/109/15/5862.full.pdf+html
(Publisher version)

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Fulltext (public)

1449076.pdf
(Publisher version), 898KB

Supplementary Material (public)

1449076_SI.pdf
(Supplementary material), 2MB

Citation

Chua, J. J. E., Butkevich, E., Worseck, J. M., Kittelmann, M., Gronborg, M., Behrmann, E., et al. (2012). Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter. Proceedings of the National Academy of Sciences of the United States of America, 109(15), 5862-5867. doi:10.1073/pnas.1113819109.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-84CB-2
Abstract
Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precis ely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntax in 1a (Stx) and Munc18, two pro- teins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabdi- tis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phos- phorylation, with a conserved site (s erine 58) being essential for bind- ing.Whenexpressedin C. elegans ,wild-typebutnotphosphorylation- de fi cient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases.