INVESTIGADORES
SESMA Juliana Ines
artículos
Título:
KIF4 mediates anterograde translocation and positioning of ribosomal constituents to axons.
Autor/es:
MARIANO BISBAL; JOSÉ WOJNACKI; DIEGO PERETTI; ANDREA ROPOLO; JULIANA SESMA; IGNACIO JAUSORO ; ALFREDO CÁCERES
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Referencias:
Lugar: Bethesda, Maryland; Año: 2009 vol. 284 p. 9489 - 9497
ISSN:
0021-9258
Resumen:
In this study, we have used a combination of biochemical and
molecular biology techniques to demonstrate that the C-termi-
nal tail domain of KIF4 directly interacts with P0, a major pro-
tein 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-bind-
ing site result in accumulation of P0 and other ribosomal pro-
teins at the cell body and in their disappearance from axons. Our
results also show one additional function for KIF4 involving an
Ezrin-Radixin-Moesin-like domain in the second coiled-coiled
region of KIF4. Expression of a KIF4 mutant lacking this domain
abolishes the clustering of ribosomal constituents and prevents
the anterograde translocation of the cell adhesion molecule L1.
Taken together, the present results suggest that by binding to P0
through its tail domain and by using its motor activity, KIF4 is
involved in the anterograde trafficking of ribosomal constitu-
ents to axons and that by means of its Ezrin-Radixin-Moesin-
like domain interacts and transports L1.