Key result
Phosphorylated GAP-43 stabilizes long actin filaments (Kd = 161 nM), whereas unphosphorylated GAP-43 reduces filament length distribution (Kd = 1.2 μM) and increases the critical concentration for polymerization.
Population
Cell-free assay using purified GAP-43 from neonatal rat brain and skeletal muscle actin from rabbit leg…
Comparison
Phosphorylated GAP-43 and unphosphorylated GAP-43 vs Actin alone
Design
Preclinical
Authors
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May regulate growth cone actin via GAP-43 phosphorylation; leaves open in vivo neuronal regeneration roles.
Spatially regulated post-translational modifications of GAP-43 within the growth cone directly influence the structure of the actin cytoskeleton.
He et al. (1997) studied this question. Phosphorylated and unphosphorylated GAP-43 vs. Actin alone was evaluated on Actin filament length and polymerization kinetics. Phosphorylated GAP-43 stabilizes long actin filaments (Kd = 161 nM), whereas unphosphorylated GAP-43 reduces filament length distribution (Kd = 1.2 μM) and increases the critical concentration for polymerization.
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