The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity.

@article{Koroll2001TheNC,
  title={The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity.},
  author={Michael Koroll and Fritz G Rathjen and Hansj{\"u}rgen Volkmer},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 14},
  pages={10646-54}
}
Neurofascin belongs to the L1 subgroup of the immunoglobulin superfamily of cell adhesion molecules and is implicated in axonal growth and fasciculation. We used yeast two-hybrid screening to identify proteins that interact with neurofascin intracellularly and therefore might link it to trafficking, spatial targeting, or signaling pathways. Here, we demonstrate that rat syntenin-1, previously published as syntenin, mda-9, or TACIP18 in human, is a neurofascin-binding protein that exhibits a… CONTINUE READING
44 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 44 extracted citations

Similar Papers

Loading similar papers…