Tripartite motif (TRIM)-containing proteins, which are defined by the presence 
of a common domain structure composed of a RING finger, one or two B-box motifs 
and a coiled-coil motif, are involved in many biological processes including 
innate immunity, viral infection, carcinogenesis, and development. Here we show 
that TRIM67, which has a TRIM motif, an FN3 domain and a SPRY domain, is highly 
expressed in the cerebellum and that TRIM67 interacts with PRG-1 and 80K-H, 
which is involved in the Ras-mediated signaling pathway. Ectopic expression of 
TRIM67 results in degradation of endogenous 80K-H and attenuation of cell 
proliferation and enhances neuritogenesis in the neuroblastoma cell line 
N1E-115. Furthermore, morphological and biological changes caused by knockdown 
of 80K-H are similar to those observed by overexpression of TRIM67. These 
findings suggest that TRIM67 regulates Ras signaling via degradation of 80K-H, 
leading to neural differentiation including neuritogenesis.