Dr. Ed Chapman and colleagues in the Chapman Lab were once again published in Nature Communications.
Their new paper, Resolving kinetic intermediates during the regulated assembly and disassembly of fusion pores, discusses findings on key kinetic intermediates that are formed during the regulated assembly and disassembly of fusion pores.
At present, little is known concerning the structure and dynamics of trans-SNARE complexes because they have been difficult to trap in distinct functional states. The major goal of the current study was to address the relationship between trans-SNARE complex assembly and fusion pore properties. To study kinetic transitions in pores, the researchers applied a newly described ND-BLM method, which affords microsecond time resolution. This approach was combined with smFRET measurements to monitor SNARE zippering.
In summary, we report key kinetic intermediates that are formed during the regulated assembly and disassembly of fusion pores. During assembly, the major Ca2+ sensor for SV exocytosis, syt1, directly regulates the occurrence, size, and dynamics of fusion pores by promoting SNARE zippering into a functionally committed state. This committed state could only be disassembled upon ATP hydrolysis by NSF, resulting in pore closure. Thus the defined, reduced, reconstituted ND-BLM system makes it possible to measure, in real time, the entire SNARE cycle, while revealing the behavior of fusion pores as they are constructed and deconstructed.
You can find more information including the full article here:
Das, D., Bao, H., Courtney, K.C. et al. Resolving kinetic intermediates during the regulated assembly and disassembly of fusion pores. Nature Communications, Vol. 11, Article number: 231 (2020). https://doi.org/10.1038/s41467-019-14072-7
Congratulations, Ed and the Chapman lab!