KIF4 mediated anterograde translocation and positioning of ribosomal constituents to developing axons

BISBAL, M., WOJNAKI, J., PERETTI, D., ROPPOLO, A., SESMA, J., JAUSORO, I., CÁCERES, A.

JOURNAL OF BIOLOGICAL CHEMISTRY

High Wire Press

Año: 2009 p. 9489 - 9497

0021-9258

In this study, we have used a combination of biochemical andmolecular biology techniques to demonstrate that the C-terminaltail domain of KIF4 directly interacts with P0, a major proteincomponent of ribosomes. Besides, in dorsal root ganglionneurons, KIF4 and P0, as well as other ribosomal constituents,colocalize in clusters distributed along axons and neuritic tips.RNA interference suppression of KIF4 or expression of KIF4variants lacking the tail domain or mutations of the ATP-bindingsite result in accumulation of P0 and other ribosomal proteinsat the cell body and in their disappearance from axons. Ourresults also show one additional function for KIF4 involving anEzrin-Radixin-Moesin-like domain in the second coiled-coiledregion of KIF4. Expression of a KIF4 mutant lacking this domainabolishes the clustering of ribosomal constituents and preventsthe anterograde translocation of the cell adhesion molecule L1.Taken together, the present results suggest that by binding to P0through its tail domain and by using its motor activity, KIF4 isinvolved in the anterograde trafficking of ribosomal constituentsto axons and that by means of its Ezrin-Radixin-Moesinlikedomain interacts and transports L1.