FIGURE

Fig. 4

ID

ZDB-FIG-241104-33

Publication

Song et al., 2024 - Thymosin β4 promotes zebrafish Mauthner axon regeneration by facilitating actin polymerization through binding to G-actin

Other Figures

All Figure Page

Back to All Figure Page

Fig. 4

The 13 N-terminal amino acids of T?4 are essential for its axon regeneration-promoting activity. a Schematic representation of the protein sequence of tmsb4x and the mutant protein sequence with a deletion of the 13 N-terminal amino acids. b 3D models of wild-type (left) and N-terminal 13 amino acids deleted (right) T?4 in complex with ?-actin, predicted by AlphaFold2. In the left image, the N-terminal 13 amino acids forming the ?-helix are highlighted in green. Below the images are the dissociation constants predicted by PRODIGY based on the 3D models. c and d Representative images (c) and statistical analysis (d) of axon regeneration in zebrafish overexpressing mutant tmsb4x with deletion of the 13 N-terminal amino acids (control, 222.5 � 45.5 ?m, n = 7; tmsb4x_D13AA, 207.1 � 23.1 ?m, n = 7). The results were assessed by an unpaired, two-tailed t test, p = 0.77. The asterisks indicate the sites of injury, and the arrows indicate the terminals of the regenerated axon. Scale bar, 100 ?m

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

This image is the copyrighted work of the attributed author or publisher, and ZFIN has permission only to display this image to its users. Additional permissions should be obtained from the applicable author or publisher of the image. Full text @ BMC Biol.