Protein changes during anterograde-to-retrograde conversion of axonally transported vesicles.

In the axon tip, cell biological mechanisms convert anterogradely transported membranous elements. To study the effects of these anterograde-to-retrograde (A-R) converting mechanisms on the electrophoretic behaviour of vesicle proteins, we compared the proteins of anterograde vesicles (before A-R conversion at the axon tip) with those of retrograde vesicles (after A-R conversion at the axon tip). The proteins in transported vesicles were pulse-labeled with [35S]methionine, and the radiolabeled vesicles were concentrated by ligating the axons-anterograde vesicles accumulate selectively on the proximal side of the ligature and retrograde vesicles accumulate on the distal side of the ligature. Analyses of vesicle proteins by polyacrylamide gel electrophoresis (SDS-PAGE) show that most of the anterograde proteins were also present in the retrograde vesicles. In addition to the conservation of these anterograde proteins in the retrograde vesicles, there were also many differences: some anterograde proteins were diminished in the retrograde vesicles, other anterograde proteins were absent from the retrograde vesicles, and the retrograde vesicles contained some new protein bands that were not present in the anterograde vesicles. These results indicate that A-R converting mechanisms modify membranous vesicle proteins in the axon tip. We propose that some of these post-translational protein modifications change the directional code on the vesicle surfaces, thereby converting anterograde membranous elements into retrograde membranous elements.