Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: effects on cell adhesion and the composition of neurite cytoskeleton and membrane.

@article{Meiri1996MutagenesisOS,
  title={Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: effects on cell adhesion and the composition of neurite cytoskeleton and membrane.},
  author={Karina F. Meiri and Joseph P. Hammang and Erik W. Dent and Emmanuel E. Baetge},
  journal={Journal of neurobiology},
  year={1996},
  volume={29 2},
  pages={213-32}
}
To investigate the molecular basis for GAP-43 function in axon outgrowth, we produced a mutant, GAP-43 (Ala41), whose interaction with calmodulin in vitro was unaffected by increasing Ca2+ concentrations, and stably transfected it into GAP-43-deficient PC12B cells. Several lines that expressed wild-type or mutant protein at levels that resembled endogenous GAP-43 expression in PC12 controls were subcloned and characterized. GAP-43 (Ala41) was significantly more extractable with Nonidet P-40 and… CONTINUE READING

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