In laboratory assays, femtomolar NAP stimulated L1-Y1229 phosphorylation at the ankyrin binding motif.
In plain wordsIn lab tests, NAP increased phosphorylation at the L1 ankyrin binding site.
- Peptide
- Davunetide
- Outcome
- IncreaseL1-Y1229 phosphorylation
- Study
n: not reported in source
Intact cells, rat brain homogenates and purified protein fragments- Outcome group
- Receptor activity and mechanism · Nervous system and cognition
- Studied dose
- Femtomolar concentrationsAs given in this study.
Source sentences
Femtomolar concentrations of NAP stimulated the phosphorylation of tyrosine-1229 (L1-Y1229) at the ankyrin binding motif of the L1 cytoplasmic domain, leading to the dissociation of L1 from ankyrin-G and the spectrin-actin cytoskeleton.
2 context sentences(design, population, supporting numbers)
L1-ankyrin-G association was studied using immunoprecipitation, Western blotting, and immunofluorescence in NIH/3T3 cells transfected with wild-type and mutated human L1 genes.
Phosphorylation of the ankyrin binding motif in the L1 cytoplasmic domain was studied after NAP treatment of intact cells, rat brain homogenates, and purified protein fragments.