A minimal domain responsible for Munc13 activity.
Munc13 proteins are essential in neurotransmitter release, controlling the priming of synaptic vesicles to a release-ready state. The sequences responsible for this priming activity are unknown. Here we identify a large alpha-helical domain of mammalian Munc13-1 that is autonomously folded and is sufficient to rescue the total arrest in neurotransmitter release observed in hippocampal neurons lacking Munc13s.
Basu
Jayeeta
J
Department of Neuroscience, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Shen
Nan
N
Dulubova
Irina
I
Lu
Jun
J
Guan
Rong
R
Guryev
Oleg
O
Grishin
Nick V
NV
Rosenmund
Christian
C
Rizo
Josep
J
D000818:Animals; D002850:Chromatography, Gel; D019295:Computational Biology; D019706:Excitatory Postsynaptic Potentials; D005089:Exocytosis / Q000235:genetics / Q000502:physiology*; D015870:Gene Expression; D006624:Hippocampus / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000378:metabolism; D009474:Neurons / Q000187:drug effects / Q000378:metabolism*; D018377:Neurotransmitter Agents / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017433:Protein Structure, Secondary / Q000235:genetics; D017434:Protein Structure, Tertiary; D051381:Rats; D013329:Structure-Activity Relationship; D013395:Sucrose / Q000494:pharmacology
D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents; C103912:Unc13a protein, rat; D013395:Sucrose