Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1.

Abstract:

:Parkin (Park2), a RING-between-RING-type E3 ubiquitin ligase, has been implicated in regulating NF-κB. Mutations in Parkin are associated with Parkinson's disease. Here we investigated the interaction of Parkin with Receptor-interacting protein kinase 1 (RIPK1) kinase, a key mediator of multiple signaling pathways activated by TNFR1 including NF-κB pathway. We report that Parkin interacts with RIPK1 and mediates K63 ubiquitination of RIPK1 on K376 in TNFR1-signaling pathway. The expression of Parkin promotes the recruitment of transforming growth factor β (TGF-β)-activated kinase 1 (TAK1), nuclear factor-κB (NF-κB) essential molecule (NEMO), Sharpin and A20 in complex I associated with TNFR1 upon TNFα stimulation. Ubiquitination of RIPK1 by Parkin increases the activation of NF-κB and mitogen-activated protein kinases (MAPKs) by promoting the phosphorylation of inhibitor of kappa B kinase (IKK)α/β and IκBα and nuclear translocation of p65. Thus, we conclude that Parkin modulates the K63 ubiquitination status of RIPK1 to promote the activation of NF-κB and MAPKs.

journal_name

Cell Death Dis

journal_title

Cell death & disease

authors

Wang Y,Shan B,Liang Y,Wei H,Yuan J

doi

10.1038/s41419-018-0770-z

subject

Has Abstract

pub_date

2018-06-28 00:00:00

pages

732

issue

7

issn

2041-4889

pii

10.1038/s41419-018-0770-z

journal_volume

9

pub_type

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