| First Author | Yaguchi H | Year | 2012 |
| Journal | J Biol Chem | Volume | 287 |
| Issue | 15 | Pages | 12050-9 |
| PubMed ID | 22337885 | Mgi Jnum | J:185071 |
| Mgi Id | MGI:5427306 | Doi | 10.1074/jbc.M111.307678 |
| Citation | Yaguchi H, et al. (2012) TRIM67 protein negatively regulates Ras activity through degradation of 80K-H and induces neuritogenesis. J Biol Chem 287(15):12050-9 |
| abstractText | 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. |
