Neuron
ArticleTargeting of neuromodulin (GAP-43) fusion proteins to growth cones in cultured rat embryonic neurons
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Cited by (66)
Growth associated protein (GAP-43): Cloning and the development of a sensitive ELISA for neurological disorders
2014, Journal of NeuroimmunologyCitation Excerpt :The amino acid sequence for GAP-43 (UniProt #P17677) is illustrated in Fig. 1a. Its localisation on the inner surface of the growth cone membrane is primarily due to a short amino terminal sequence comprising of the first ten amino acids of the N-terminus. Cysteines 3 and 4 are crucial for the membrane association (Zuber et al., 1989; Liu et al., 1991). Therefore, when producing the soluble recombinant GAP-43 protein we omitted the membrane binding region and used only amino acids 11–238 (Val–Ala) of GAP-43 to allow for its secretion during the expression phase of protein production.
Synaptotagmin-Mediated Bending of the Target Membrane Is a Critical Step in Ca<sup>2+</sup>-Regulated Fusion
2009, CellCitation Excerpt :We next determined whether the localization of syt to vesicles is required for its function. C2A-C2B was fused to the N-terminal membrane-targeting motif of GAP-43 (Figure 6A, lower), a protein that is anchored to the inner leaflet of the plasma membrane via two palmitoylated cysteines (Liu et al., 1991). This fusion construct (GAP43-C2A-C2B) was indeed targeted to the plasma membrane of cells (Figures 6A and S16) and rescued rapid synaptic transmission in syt I KO neurons (Figures 6B–6D).
A Live Cell, Image-Based Approach to Understanding the Enzymology and Pharmacology of 2-Bromopalmitate and Palmitoylation
2006, Methods in EnzymologyCitation Excerpt :For this kinase, the N‐terminal glycine is consistently modified by myristate, but the adjacent cysteine residue is modified most frequently by palmitate but also by palmitoleate, stearate, or oleate (Liang et al., 2004) with a frequency of residence on the protein that is apparently related to their abundance. The involvement of palmitoylation in development is exemplified by GAP43 and paralemmin, which are localized to filopodia and growth cones (Liu et al., 1991; Skene and Virag, 1989; Strittmatter, 1991, 1992; Zuber et al., 1989a,b) where each has been shown to influence the formation of filopodia and the branching of dendrites and axons. Interestingly, it has also been shown that simply expressing the palmitoylation motifs of these proteins fused to GFP is sufficient to induce the changes seen when overexpressing the native forms of GAP43 and paralemmin (Gauthier‐Campbell et al., 2004).
A multifunctional domain of the calcium-responsive transactivator (CREST) that inhibits dendritic growth in cultured neurons
2005, Journal of Biological ChemistryCitation Excerpt :Cell Cultures and Transfection—PC12 and HEK293 cells were cultured and transfected by polyethyleneimine and calcium phosphate method, respectively, as described previously (3). Rat embryonic cortical neurons were cultured as described previously (10). The cortices from day 17 embryos of Sprague-Dawley rat were dissected and dissociated by trituration.
Optimized protocol for biolistic transfection of brain slices and dissociated cultured neurons with a hand-held gene gun
1999, Journal of Neuroscience MethodsA key role for GAP-43 in the retinotectal topographic organization
1999, Experimental Neurology