Characterization of a novel tumor necrosis factor-alpha-induced endothelial primary response gene.

Wolf, F W; Marks, Rebecca A.; Sarma, Vidya; Byers, Mary G.; Katz, Ronald W.; Shows, T.B.; Dixit, Vishva M.

doi:10.1016/s0021-9258(18)48432-3

Cited by 76 publications

(17 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, each BACURD in the same cell might control levels of RhoA in a specific population and/or regulate a distinct RhoA-controlled signaling pathway. hBACURD2 was originally identified as one of the tumor necrosis factor (TNF)-induced genes in human endothelial cells (Wolf et al, 1992). Microarray data mined from the Genomics Institute of the Novartis Research Foundation (http://biogps.gnf.org) suggest that BACURD2 are ubiquitously expressed in various human and mouse tissues, while transcripts of BACURD1 are more enriched in oocytes, germ cells, and some brain tissues.…”

Section: Differential Functions Of Different Bacurd Family Members In Vertebratesmentioning

confidence: 99%

Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement

et al. 2009

View full text Add to dashboard Cite

Cul3, a Cullin family scaffold protein, is thought to mediate the assembly of a large number of SCF (Skp1-Cullin1-F-box protein)-like ubiquitin ligase complexes through BTB domain substrate-recruiting adaptors. Cul3 controls early embryonic development in several genetic models through mechanisms not understood. Very few functional substrate/adaptor pairs for Cul3 ubiquitin ligases have been identified. Here, we show that Cul3 knockdown in human cells results in abnormal actin stress fibers and distorted cell morphology, owing to impaired ubiquitination and degradation of small GTPase RhoA. We identify a family of RhoA-binding BTB domain adaptors conserved from insects to mammals, designated BACURDs. BACURDs form ubiquitin ligase complexes, which selectively ubiquitinate RhoA, with Cul3. Dysfunction of the Cul3/BACURD complex decreases cell migration potential and impairs RhoA-mediated convergent extension movements during Xenopus gastrulation. Our studies reveal a previously unknown mechanism for controlling RhoA degradation and regulating RhoA function in various biological contexts, which involves a Cul3/BACURD ubiquitin ligase complex.

show abstract

Section: Differential Functions Of Different Bacurd Family Members In Vertebratesmentioning

confidence: 99%

Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement

et al. 2009

View full text Add to dashboard Cite

show abstract

“…TNFAIP1can be activated by TNFα and IL-6 and it plays significant roles in many human diseases (Wolf, Marks, & Sarma, 1992). TNFAIP1 is abnormally expressed in various cancers (Zhou, Li, & Zhang, 2013;Zhu et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Effects of XIST/miR‐137 axis on neuropathic pain by targeting TNFAIP1 in a rat model

Zhao

Xia

et al. 2017

Journal Cellular Physiology

View full text Add to dashboard Cite

Non-coding RNAs have been reported to participate in the pathophysiology of neuropathic pain. The objective of our study was to investigate the biological role of XIST in neuropathic pain development. In our study, we identify and validate that lncRNA XIST was markedly increased and miR-137 was significantly decreased in chronic constriction injury (CCI) rats. XIST silencing alleviated pain behaviors including both mechanical and thermal hyperalgesia in the CCI rats. XIST was predicted to interact with miR-137 by bioinformatics technology and dual-luciferase reporter assays confirmed the correlation between XIST and miR-137. miR-137 was negatively modulated by XIST and upregulation of miR-137 greatly reduced neuropathic pain development in CCI rats. Moreover, we observed that tumor necrosis factor alpha-induced protein 1 (TNFAIP1) was enhanced in CCI rats and 3'-untranslated region (UTR) of TNFAIP1 was exhibited to be a target of miR-137 by bioinformatics prediction. TNFAIP1 can act as a crucial inflammation regulator by activating NF-kB activity. Overexpression of miR-137 significantly suppressed TNFAIP1 both in vitro and in vivo. Furthermore, upregulation of XIST reversed the inhibitory role of miR-137 in neuropathic pain development by inhibiting TNFAIP1. In conclusion, our current study indicates that XIST can positively regulate neuropathic pain in rats through regulating the expression of miR-137 and TNFAIP1. Our results imply that XIST/miR-137/TNFAIP1 axis may serve as a novel therapeutic target in neuropathic pain.

show abstract

“…Tumor necrosis factor a-induced protein 1 (TNFAIP1), also known as B12 or BACURD2, was initially identified as a tumor necrosis factor alpha (TNFa)-and lipopolysaccharide (LPS)-induced gene in umbilical vein endothelial cells [3]. In mammals, the amino acid sequences of TNFAIP1 are highly similar to polymerase delta-interacting protein 1 (PDIP1) and potassium channel tetramerization domain containing 10 (KCTD10), where all of them contain a conserved BR-C, ttk, and bab (BTB)/Pox virus and zinc finger (POZ) domain and a proliferating cell nuclear antigen (PCNA) binding motif [4].…”

Section: Introductionmentioning

confidence: 99%

Tumor necrosis factor α-induced protein 1 as a novel tumor suppressor through selective downregulation of CSNK2B blocks nuclear factor-κB activation in hepatocellular carcinoma

et al. 2020

View full text Add to dashboard Cite

Background: Tumor necrosis factor a-induced protein 1 (TNFAIP1) is frequently downregulated in cancer cell lines and promotes cancer cell apoptosis. However, its role, clinical significance and molecular mechanisms in hepatocellular carcinoma (HCC) are unknown. Methods: The expression of TNFAIP1 in HCC tumor tissues and cell lines was measured by Western blot and immunohistochemistry. The effects of TNFAIP1 on HCC proliferation, apoptosis, metastasis, angiogenesis and tumor formation were evaluated by Cell Counting Kit-8 (CCK8), Terminal deoxynucleotidyl transferase dUTP Nick-End Labeling (TUNEL), transwell, tube formation assay in vitro and nude mice experiments in vivo. The interaction between TNFAIP1 and CSNK2B was validated by liquid chromatography-tandem mass spectrometry (LC-MS/MS), Co-immunoprecipitation and Western blot. The mechanism of how TNFAIP1 regulated nuclear factor-kappaB (NF-kB) pathway was analyzed by dual-luciferase reporter, immunofluorescence, quantitative Real-time polymerase chain reaction (RT-qPCR) and Western blot. Findings: The TNFAIP1 expression is significantly decreased in HCC tissues and cell lines, and negatively correlated with the increased HCC histological grade. Overexpression of TNFAIP1 inhibits HCC cell proliferation, metastasis, angiogenesis and promotes cancer cell apoptosis both in vitro and in vivo, whereas the knockdown of TNFAIP1 in HCC cell displays opposite effects. Mechanistically, TNFAIP1 interacts with CSNK2B and promotes its ubiquitin-mediated degradation with Cul3, causing attenuation of CSNK2B-dependent NF-kB trans-activation in HCC cell. Moreover, the enforced expression of CSNK2B counteracts the inhibitory effects of TNFAIP1 on HCC cell proliferation, migration, and angiogenesis in vitro and in vivo. Interpretation: Our results support that TNFAIP1 can act as a tumor suppressor of HCC by modulating TNFAIP1/CSNK2B/NF-kB pathway, implying that TNFAIP1 may represent a potential marker and a promising therapeutic target for HCC.

show abstract

Characterization of a novel tumor necrosis factor-alpha-induced endothelial primary response gene.

Cited by 76 publications

References 57 publications

Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement

Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement

Effects of XIST/miR‐137 axis on neuropathic pain by targeting TNFAIP1 in a rat model

Tumor necrosis factor α-induced protein 1 as a novel tumor suppressor through selective downregulation of CSNK2B blocks nuclear factor-κB activation in hepatocellular carcinoma

Contact Info

Product

Resources

About