Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter.
Proc Natl Acad Sci U S A
; 109(15): 5862-7, 2012 Apr 10.
Article
em En
| MEDLINE
| ID: mdl-22451907
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.
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Base de dados:
MEDLINE
Assunto principal:
Transporte Axonal
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Neuropeptídeos
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Cinesinas
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Proteínas de Caenorhabditis elegans
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Proteínas Adaptadoras de Transdução de Sinal
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Sintaxina 1
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Proteínas do Tecido Nervoso
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article