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FEBS Lett. 2018 May;592(9):1575-1588. doi: 10.1002/1873-3468.13039. Epub 2018 Apr 10.

PME-1 is regulated by USP36 in ERK and Akt signaling pathways.

Author information

1
Department of Biomedical Science, CHA University, Seongnam-Si, Gyeonggi-Do, Korea.

Abstract

Deubiquitinating enzymes (DUBs) play an important role in the ubiquitin-proteasome system (UPS) by eliminating ubiquitins from substrates and inhibiting proteasomal degradation. Protein phosphatase methylesterase 1 (PME-1) inactivates protein phosphatase 2A (PP2A) and enhances the ERK and Akt signaling pathways, which increase cell proliferation and malignant cell transformation. In this study, we demonstrate that USP36 regulates PME-1 through its deubiquitinating enzyme activity. USP36 increases PME-1 stability, and depletion of USP36 decreases the PME-1 expression level. Furthermore, we demonstrate that USP36 promotes the ERK and Akt signaling pathways. In summary, it is suggested that USP36 regulates PME-1 as a DUB and participates in the ERK and Akt signaling pathways.

KEYWORDS:

Akt signaling pathway; ERK signaling pathway; Malignant transformation; USP36; deubiquitinating enzyme; ubiquitination

PMID:
29577269
DOI:
10.1002/1873-3468.13039
[Indexed for MEDLINE]
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