Direct Interaction of the Rat unc-13 Homologue Munc13-1 with the N Terminus of Syntaxin*
- A. Betz, M. Okamoto, F. Benseler, N. Brose
- Biology, ChemistryJournal of Biological Chemistry
- 24 January 1997
It is demonstrated by three independent methods that the C terminus of Munc13-1 interacts directly with a putative coiled coil domain in the N-terminal part of syntaxin, indicating that unc-13-related proteins may indeed be involved in the mediation or regulation of synaptic vesicle exocytosis by modulating or regulating core complex formation.
Munc13-1 C1 Domain Activation Lowers the Energy Barrier for Synaptic Vesicle Fusion
- Jayeeta Basu, A. Betz, N. Brose, Christian Rosenmund
- BiologyJournal of Neuroscience
- 31 January 2007
This work proposes a PKC analogous two-state model of regulation of Munc13s, in which the basal state of Mun c13s is disinhibited by C1 domain activation into a state of facilitated vesicle release, regardless of whether the release is spontaneous or action potential triggered.
Munc13‐1 acts as a priming factor for large dense‐core vesicles in bovine chromaffin cells
- U. Ashery, F. Varoqueaux, J. Rettig
- BiologyEMBO Journal
- 17 July 2000
It is concluded that Munc13‐1 acts as a priming factor by accelerating the rate constant of vesicle transfer from a Pool of docked, but unprimed vesicles to a pool of release‐competent, primed vesicular fusion.
Differential expression of two novel Munc13 proteins in rat brain.
- I. Augustin, A. Betz, C. Herrmann, T. Jo, N. Brose
- BiologyBiochemical Journal
- 1 February 1999
The results characterize Munc13 proteins as a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release.
Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals
- N. Brose, A. Betz, Heike Wegmeyer
- Biology, Computer ScienceCurrent Opinion in Neurobiology
- 1 June 2004
EphA4-dependent axon guidance is mediated by the RacGAP alpha2-chimaerin.
- Heike Wegmeyer, J. Egea, A. Betz
- BiologyNeuron
- 2007
The results reveal an alpha-chimaerin-dependent signaling pathway downstream of EphA4, which is essential for axon guidance decisions and neuronal circuit formation in vivo.
Model for the Exceptional Reactivity of Peroxiredoxins 2 and 3 with Hydrogen Peroxide
- P. Nagy, A. Karton, C. Winterbourn
- Chemistry, BiologyJournal of Biological Chemistry
- 8 March 2011
The results provide strong evidence for a vital role of ArgI in activating the peroxide that also involves H-bonding to ArgII, which could explain the exceptional reactivity of peroxiredoxins toward H2O2 and may have wider implications for protein thiol reactivity toward peroxides.
...
...