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Open syntaxin overcomes synaptic transmission defects in diverseC. elegansexocytosis mutants
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SummaryAssembly of SNARE complexes that mediate neurotransmitter release requires opening of a ‘closed’ conformation of UNC-64/syntaxin. Rescue ofunc-13/Munc13phenotypes by overexpressed open UNC-64/syntaxin suggested a specific function of UNC-13/Munc13 in opening UNC-64/ syntaxin. Here, we revisit the effects of openunc-64/syntaxin by generating knockin (KI) worms. The KI animals exhibited enhanced spontaneous and evoked exocytosis compared to wild-type animals. Unexpectedly, the open syntaxin KI partially suppressed exocytosis defects of various mutants, includingsnt-1/synaptotagmin,unc-2/P/Q/N-type Ca2+channel alpha-subunit, andunc-31/CAPS in addition tounc-13/Munc13 andunc-10/RIM, and enhanced exocytosis intom-1/Tomosyn mutants. However, open syntaxin aggravated the defects ofunc-18/Munc18 mutants. Correspondingly, open syntaxin partially bypasses the requirement of Munc13 but not Munc18 for liposome fusion. Our results show that facilitating opening of syntaxin enhances exocytosis in a wide range of genetic backgrounds, and may provide a general means to enhance synaptic transmission in normal and disease states.
Cold Spring Harbor Laboratory
Title: Open syntaxin overcomes synaptic transmission defects in diverseC. elegansexocytosis mutants
Description:
SummaryAssembly of SNARE complexes that mediate neurotransmitter release requires opening of a ‘closed’ conformation of UNC-64/syntaxin.
Rescue ofunc-13/Munc13phenotypes by overexpressed open UNC-64/syntaxin suggested a specific function of UNC-13/Munc13 in opening UNC-64/ syntaxin.
Here, we revisit the effects of openunc-64/syntaxin by generating knockin (KI) worms.
The KI animals exhibited enhanced spontaneous and evoked exocytosis compared to wild-type animals.
Unexpectedly, the open syntaxin KI partially suppressed exocytosis defects of various mutants, includingsnt-1/synaptotagmin,unc-2/P/Q/N-type Ca2+channel alpha-subunit, andunc-31/CAPS in addition tounc-13/Munc13 andunc-10/RIM, and enhanced exocytosis intom-1/Tomosyn mutants.
However, open syntaxin aggravated the defects ofunc-18/Munc18 mutants.
Correspondingly, open syntaxin partially bypasses the requirement of Munc13 but not Munc18 for liposome fusion.
Our results show that facilitating opening of syntaxin enhances exocytosis in a wide range of genetic backgrounds, and may provide a general means to enhance synaptic transmission in normal and disease states.
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