TRIM67 protein negatively regulates Ras activity through degradation of 80K-H and induces neuritogenesis.

The Journal of Biological Chemistry
Hiroaki YaguchiShigetsugu Hatakeyama

Abstract

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.

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Citations

Apr 30, 2014·The Journal of Cell Biology·Cortney C WinkleStephanie L Gupton
Feb 8, 2013·Biochimica Et Biophysica Acta·Ulf Strauss, Anja U Bräuer
Oct 27, 2016·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·Song GaoBei Lin
Nov 7, 2019·Stem Cells and Development·Valentina V Nenasheva, Vyacheslav Z Tarantul
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Dec 11, 2019·The Journal of Cell Biology·Nicholas P BoyerStephanie L Gupton
Dec 31, 2020·Molecular Biology of the Cell·Shalini MenonStephanie L Gupton

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