Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity.

@article{Nagiec1995EachDO,
  title={Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity.},
  author={E E Nagiec and Audrey M Bernstein and Sidney W Whiteheart},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 49},
  pages={29182-8}
}
N-Ethylmaleimide-sensitive fusion protein (NSF) has been shown to be involved in numerous intracellular transport events. In an effort to understand the basic mechanism of NSF in vesicle-target membrane fusion events, we have examined the role that each of its three domains play in how NSF interacts with the SNAP.SNARE complex. Mutagenesis of the first ATP-binding domain (D1, amino acids 206-477) demonstrates that nucleotide binding by this domain is required for 20 S particle assembly. A… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 41 extracted citations

Similar Papers

Loading similar papers…