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• W2060313939 abstract "Lysophosphatidic acid (LPA) is a bioactive phospholipid and binds to its receptors, a family of G protein-coupled receptors (GPCR), which initiates multiple signaling cascades and leads to activation of several transcription factors, including NF-κB. Although LPA-induced signaling pathways have been intensively investigated, the molecular mechanism by which LPA activates NF-κB is not fully defined. In this work, we found that β-arrestin 2, but not β-arrestin 1, is required for LPA-induced NF-κB activation and interlukin-6 expression. Mechanistically, we found that β-arrestin 2 associated with CARMA3, a scaffold protein that plays an essential role in GPCR-induced NF-κB activation, suggesting that β-arrestin 2 may recruit CARMA3 to LPA receptors. Although β-arrestin 2 deficiency did not affect LPA-induced IKKα/β phosphorylation, it impaired LPA-induced IKK kinase activity, which is consistent with our previous findings that CARMA3 is required for IKKα/β activation but not for the inducible phosphorylation of IKKα/β. Together, our results provide the genetic evidence that β-arrestin 2 serves as a positive regulator in NF-κB signaling pathway by connecting CARMA3 to GPCRs." @default.
• W2060313939 created "2016-06-24" @default.
• W2060313939 creator A5047717810 @default.
• W2060313939 creator A5049585978 @default.
• W2060313939 date "2008-11-04" @default.
• W2060313939 modified "2023-09-26" @default.
• W2060313939 title "β-Arrestin 2 is required for lysophosphatidic acid-induced NF-κB activation" @default.
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• W2060313939 doi "https://doi.org/10.1073/pnas.0802701105" @default.
• W2060313939 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2579382" @default.
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