ArticlePloS one2011
The ubiquitin-like protein PLIC-1 or ubiquilin 1 inhibits TLR3-Trif signaling.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Ubiquilin 1 Inhibits intracellular proliferation of Salmonella enterica serovar Typhimurium through Xenophagy.Genes & genomics · 2026Article
- Knockdown of Tlr3 in dorsal striatum reduces ethanol consumption and acute functional tolerance in male mice.Brain, behavior, and immunity · 2024Article
- Supramolecular Complexes in Cell Death and Inflammation and Their Regulation by Autophagy.Frontiers in cell and developmental biology · 2019Review
- Article
- Studying the Effect of Downregulating Autophagy-Related Gene LC3 on TLR3 Apoptotic Pathway Mediated by dsRNA in Hepatocellular Carcinoma Cells.Cancer research and treatment · 2017Article
- Identification of novel human kinases that suppress hepatitis C virus infection.Journal of viral hepatitis · 2014Article
- MCPIP1 restricts HIV infection and is rapidly degraded in activated CD4+ T cells.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The TREX1 C-terminal region controls cellular localization through ubiquitination.The Journal of biological chemistry · 2013Article
- Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization.Molecules and cells · 2013Article
- Mapping of Chikungunya virus interactions with host proteins identified nsP2 as a highly connected viral component.Journal of virology · 2012Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundThe innate immune responses to virus infection are initiated by either Toll-like receptors (TLR3/7/8/9) or cytoplasmic double-stranded RNA (dsRNA)-recognizing RNA helicases RIG-I and MDA5. To avoid causing injury to the host, these signaling pathways must be switched off in time by negative regulators. METHODOLOGY/PRINCIPAL
findingsThrough yeast-two hybrid screening, we found that an ubiquitin-like protein named protein linking integrin-associated protein to cytoskeleton 1(PLIC-1 or Ubiquilin 1) interacted with the Toll/interleukin-1 receptor (TIR) domain of TLR4. Interestingly, PLIC-1 had modest effect on TLR4-mediated signaling, but strongly suppressed the transcriptional activation of IFN-β promoter through the TLR3-Trif-dependent pathway. Concomitantly, reduction of endogenous PLIC-1 by short-hairpin interfering RNA (shRNA) enhanced TLR3 activation both in luciferase reporter assays as well as in new castle disease virus (NDV) infected cells. An interaction between PLIC-1 and Trif was confirmed in co-immunoprecipitation (Co-IP) and GST-pull-down assays. Subsequent confocal microscopic analysis revealed that PLIC-1 and Trif colocalized with the autophagosome marker LC3 in punctate subcellular structures. Finally, overexpression of PLIC-1 decreased Trif protein abundance in a Nocodazole-sensitive manner.
conclusionsOur results suggest that PLIC-1 is a novel inhibitor of the TLR3-Trif antiviral pathway by reducing the abundance of Trif.
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Registered trials
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