SIAH ubiquitin E3 ligases as modulators of inflammatory gene expression

Schmitz, M. Lienhard; Dreute, Jan; Pfisterer, Maximilian; Günther, Stefan; Chillappagari, Shashi

doi:10.1016/j.heliyon.2022.e09029

Cited by 6 publications

(3 citation statements)

References 37 publications

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“…8C ). This behavior suggests a mutual compensatory mechanism for both adapter proteins, a feature that is frequently observed in multiprotein complexes ( 58 , 59 ). These blots and their quantitative analysis also showed that the double knockdown led to a slight but significant decrease in the levels of viral proteins (M1, NS1, and NP) ( Fig.…”

Section: Resultsmentioning

confidence: 73%

Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine 108 Controls Its Multimerization State and Functional Association with the STRIPAK Complex

Liu

Weber

Linne

et al. 2023

mBio

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Section: Resultsmentioning

confidence: 73%

Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine 108 Controls Its Multimerization State and Functional Association with the STRIPAK Complex

Liu

Weber

Linne

et al. 2023

mBio

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“… 16 , 17 In contrast, SIAH2 is widely expressed in different cell types and participates in the ubiquitination and degradation of multiple substrates, such as PHD3, HIPK2, p300, Tip60 and PRCAF, thereby regulating cellular processes, including proliferation, invasion, and migration. 18 , 19 , 20 SIAH2 has been identified as a promoter of various human malignant tumours, including prostate cancer, 21 lung cancer, 22 gastric cancer 23 and HCC. 24 SIAH2 also exhibits tumour‐inhibitory effects in HCC by the degradation of oncoproteins through the proteasome pathway.…”

Section: Introductionmentioning

confidence: 99%

“…The mRNA and protein levels of SIAH1 exert tumour‐inhibitory effects and have been reported as downregulated in cancer 16,17 . In contrast, SIAH2 is widely expressed in different cell types and participates in the ubiquitination and degradation of multiple substrates, such as PHD3, HIPK2, p300, Tip60 and PRCAF, thereby regulating cellular processes, including proliferation, invasion, and migration 18–20 . SIAH2 has been identified as a promoter of various human malignant tumours, including prostate cancer, 21 lung cancer, 22 gastric cancer 23 and HCC 24 .…”

Section: Introductionmentioning

confidence: 99%

SIAH2 suppresses c‐JUN pathway by promoting the polyubiquitination and degradation of HBx in hepatocellular carcinoma

Hu,

Liu,

Liu

et al. 2024

J Cellular Molecular Medi

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As an important protein encoded by hepatitis B virus (HBV), HBV X protein (HBx) plays an important role in the development of hepatocellular carcinoma (HCC). It has been shown that seven in absentia homologue 1 (SIAH1) could regulates the degradation of HBx through the ubiquitin‐proteasome pathway. However, as a member of SIAH family, the regulatory effects of SIAH2 on HBx remain unclear. In this study, we first confirmed that SIAH2 could reduce the protein levels of HBx depending on its E3 ligase activity. Moreover, SIAH2 interacted with HBx and induced its K48‐linked polyubiquitination and proteasomal degradation. Furthermore, we provided evidence that SIAH2 inhibits HBx‐associated HCC cells proliferation by regulating HBx. In conclusion, our study identified a novel role for SIAH2 in promoting HBx degradation and SIAH2 exerts an inhibitory effect in the proliferation of HBx‐associated HCC through inducing the degradation of HBx. Our study provides a new idea for the targeted degradation of HBx and may have great huge significance into providing novel evidence for the targeted therapy of HBV‐infected HCC.

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SIAH3 is frequently epigenetically silenced in cancer and regulates mitochondrial metabolism

Deutschmeyer,

Schlaudraff,

Walesch

et al. 2024

Intl Journal of Cancer

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Of the seven in absentia homologue (SIAH) family, three members have been identified in the human genome. In contrast to the E3 ubiquitin ligase encoding SIAH1 and SIAH2, little is known on the regulation and function of SIAH3 in tumorigenesis. In this study, we reveal that SIAH3 is frequently epigenetically silenced in different cancer entities, including cutaneous melanoma, lung adenocarcinoma and head and neck cancer. Low SIAH3 levels correlate with an impaired survival of cancer patients. Additionally, induced expression of SIAH3 reduces cell proliferation and induces cell death. Functionally, SIAH3 negatively affects cellular metabolism by shifting cells form aerobic oxidative phosphorylation to glycolysis. SIAH3 is localized in the mitochondrion and interacts with proteins involved in mitochondrial ribosome biogenesis and translation. We also report that SIAH3 interacts with ubiquitin ligases, including SIAH1 or SIAH2, and is degraded by them. These results suggest that SIAH3 acts as an epigenetically controlled tumor suppressor by regulating cellular metabolism through the inhibition of oxidative phosphorylation.

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SIAH ubiquitin E3 ligases as modulators of inflammatory gene expression

Cited by 6 publications

References 37 publications

Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine 108 Controls Its Multimerization State and Functional Association with the STRIPAK Complex

Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine 108 Controls Its Multimerization State and Functional Association with the STRIPAK Complex

SIAH2 suppresses c‐JUN pathway by promoting the polyubiquitination and degradation of HBx in hepatocellular carcinoma

SIAH3 is frequently epigenetically silenced in cancer and regulates mitochondrial metabolism

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