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

Item Type:Article
Title:Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter
Creators Name:Chua, J.J.E., Butkevich, E., Worseck, J.M., Kittelmann, M., Gronborg, M., Behrmann, E., Stelzl, U., Pavlos, N.J., Lalowski, M.M., Eimer, S., Wanker, E.E., Klopfenstein, D.R. and Jahn, R.
Abstract:Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins 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 Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient 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.
Keywords:Fasciculation and Elongation Protein zeta 1, Transport Defect, Cargo Aggregation, Animals
Source:Proceedings of the National Academy of Sciences of the United States of America
Publisher:National Academy of Sciences
Page Range:5862-5867
Date:10 April 2012
Official Publication:https://doi.org/10.1073/pnas.1113819109
PubMed:View item in PubMed

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