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Ubiquitin-specific protease 14 regulates LPS-induced inflammation by increasing ERK1/2 phosphorylation and NF-κB activation.

Abstract：

:Persistent activation of nuclear factor B (NF-κB) is very important in the modulation of macrophages cellular response to microbial infections. The deubiquitinase USP14, which is critical for ubiquitin-mediated proteasomal degradation of proteins, is known to be involved in cancer, neurological diseases, and aging. However, the mechanism by which USP14 regulates inflammation remains unclear. Here, we demonstrated that decreasing the deubiquitinase activity of USP14 resulted in reduced lipopolysaccharides (LPS)-mediated tumor necrosis factor-α (TNF-α) and interleukin (IL)-6 release in THP-1 and RAW264.7 cells. Meanwhile, USP14 knockdown by siRNA showed the same effects, with no cytotoxicity in THP-1 cells. Moreover, inhibiting the deubiquitinase activity of USP14 or USP14 knockdown resulted in decreased ERK1/2 and IκBα phosphorylation, increased amounts of the NF-κB inhibitor IκBα, and reduced NF-κB p65 transport from the cytoplasm into nucleus. These findings suggested that USP14 induces NF-κB activity and ERK1/2 phosphorylation triggered by microbial infection.

journal_name

Mol Cell Biochem

journal_title

Molecular and cellular biochemistry

authors

Liu N,Kong T,Chen X,Hu H,Gu H,Liu S,Chen X,Yang Q,Li A,Xiong X,Zhang Z

doi

10.1007/s11010-017-2978-0

subject

Has Abstract

pub_date

2017-07-01 00:00:00

pages

87-96

issue

1-2

eissn

0300-8177

issn

1573-4919

pii

10.1007/s11010-017-2978-0

journal_volume

431

pub_type

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