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Fig. 5. Region n of domain A displays a Golgi-specifying activity when appended to the palmitoylation signal of GAP-43. GFP fusion proteins containing either region n, domain A, the palmitoylated N-terminal domain of GAP-43, or a combination of region n and the N-terminal domain of GAP-43 were transfected in HeLa cells. (A) Conventional fluorescence microscopy image for GFP alone as a control and for each construct. (B) Weakly expressing cells were classified according to the relative distribution of the GFP fusion proteins between the Golgi complex and the plasma membrane. The presence of region n appended to the N-terminal domain of GAP-43 resulted in a higher proportion of fusion protein at the Golgi complex, compared to the protein with the N-terminal domain of GAP-43 alone. G>PM, mainly localized to the Golgi complex; G~PM, equally distributed between the Golgi complex and the plasma membrane; PM>G, mainly localized to the plasma membrane. Bar, 10 µm.





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