KIF4 mediates anterograde translocation and positioning of ribosomal constituents to axons.

BISBAL MARIANO; WOJNACKI JOSÉ; JAUSORO I; PERETTI DIEGO; ROPOLO ANDREA; SESMA JULIANA; CÁCERES ALFREDO

ASBMB

Lugar: USA; Año: 2009 vol. 284 p. 9489 - 9489

font size="2" face="WarnockPro-Semibold"> In this study, we have used a combination of biochemical and molecular biology techniques to demonstrate that the C-terminal tail domain of KIF4 directly interacts with P0, a major protein component of ribosomes. Besides, in dorsal root ganglion neurons, 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 KIF4 variants lacking the tail domain or mutations of the ATP-binding site result in accumulation of P0 and other ribosomal proteins at the cell body and in their disappearance from axons. Our results also show one additional function for KIF4 involving an