SENP1 Proteine (SENP1)

Human SUMO1/sentrin Specific Peptidase 1 (SENP1) Interaktionspartner

1. Study revealed a significant decrease in the expression of SUMO1 specific peptidase 1 (SENP1) in osteosarcoma tissues and osteosarcoma cell lines, and SENP1 expression was much lower in osteosarcoma stem cells than in noncancer stem cells.

2. KLF15 is a critical regulator of pulmonary endothelial homeostasis via repression of endothelial Arg2 expression. KLF15 abundance and nuclear compartmentalization are regulated by SUMOylation/deSUMOylation-a hypoxia-sensitive process that is controlled by SENP1.

3. Results in this present study showed that SENP1 was a risk factor for poor non-small cell lung cancer prognosis. And also demonstrated that the overexpression of SENP1 in non-small cell lung cancer was related to chemotherapy resistance.

4. SENP1 is a crucial c-Myc deSUMOylating enzyme that positively regulates c-Myc's stability and activity.

5. endothelial SENP1-mediated SUMOylation drives graft arteriosclerosis by regulating the synergistic effect of GATA2 and NF-kappaB and consequent endothelial dysfunction.

6. Results showed that the expression of SENP1 was remarkably upregulated in osteosarcoma cells (OS) cells. SENP1 positively regulated HIF-1alpha expression level in the setting of hypoxic; subsequently, its depletion markedly ameliorated VEGF production triggered by hypoxia.

7. These results suggest that the miR-133a-3p-SENP1 axis might play a role in cell proliferation and cell cycle regulation of colorectal cancer cells.

8. Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ.

9. miR-185 was significantly downregulated in RCC tissues and cell lines. SENP1 was a direct target of miR-186, and SENP1 mRNA expression was reversely correlated with miR-186 in RCC tissues.

10. Treatment of cells with streptonigrin resulted in increased global SUMOylation levels and reduced level of hypoxia inducible factor alpha (HIF1alpha). These findings inform both the design of SENP1 targeting strategy and the modification of streptonigrin to improve its efficacy for possible future clinical use.

11. SENP1 promotes cell proliferation and disease progression in clear cell renal cell carcinoma, possibly through deSUMOylating and stabilizing HIF-1alpha, leading to increased expression of key glycolytic enzymes and enhanced glycolytic flux.

12. Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region.

13. GATA1 is an essential downstream target of SENP1 and that the differential expression and response of GATA1 and Bcl-xL are a key mechanism underlying chronic mountain sickness pathology.

14. miRNA1236 regulates hypoxia-induced epithelial-mesenchymal transformation and metastasis by repressing HDAC3 and SENP1 expression.

15. SENP1 deSUMOylated SMAD4 to promote EMT via up-regulating E-cadherin in prostate cancer cells. Therefore, SENP1 is a potential target for treatment of advanced prostate cancer.

16. The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.

17. this study elucidated that SENP1 is essential for triple-negative breast cancer cell proliferation and migration in vitro, as well as tumor formation and metastasis in vivo

18. Hepatocellular carcinoma cells express a high level of Senp1 which is induced by HGF/c-Met signals. Senp1 silencing reduces the HGF-induced proliferation and migration of HCC cells, induces HCC cell apoptosis and growth arrest, and epithelial-to-mesenchymal transition, with increase of E-cadherin and ZO-1 expression, decrease of fibronectin and N-cadherin expression.

19. a significant role of SENP1 in the regulation of cell migration and invasion in neuroblastoma

20. A key role for SENP1 in astrocytoma development and apoptosis.SENP1 inhibition promotes cell apoptosis by regulating NF-kappa B/Akt signaling pathways.

Mouse (Murine) SUMO1/sentrin Specific Peptidase 1 (SENP1) Interaktionspartner

1. endothelial SENP1-mediated SUMOylation drives graft arteriosclerosis by regulating the synergistic effect of GATA2 and NF-kappaB and consequent endothelial dysfunction.

2. knockdown of SENP1 augments the ability of Shh to sustain the proliferation of cerebellar granule cell precursors, demonstrating the physiological significance of the negative regulation of Shh signaling by SENP1.

3. SUMO1 conjugation of RB and Lamin A/C is modulated by the SUMO protease SENP1 and that sumoylation of both proteins is required for their interaction.

4. SENP1 plays a neuroprotective role in ischemia/reperfusion injury.

5. a novel negative feedback loop mediated by STAT3-SOCS3, which is tightly controlled by SENP1 via de-SUMOylation of protein tyrosine phosphatase 1B (PTP1B), in IFN-gamma signaling, is reported.

6. SENP1 deletion in adipocytes causes Type 1 diabetes mellitus via enhanced SUMOylation of NEMO, leading to increased NF-kappaB activity, cytokine production and pancreatic inflammation.

7. results of the present study are of both theoretical and therapeutic significance to explore the potential roles of SENP1 under IH condition and elucidated the mechanisms underlying microglial survival and activation

8. A role for islet SENP1 as a regulator of in vivo glucose homeostasis was demonstrated by the tissue-selective and inducible knockout of this enzyme.

9. SENP1 up-regulation in diseased heart is mediated via calcineurin-NFAT/MEF2C-PGC-1alpha pathway.

10. SENP1 deficiency exacerbates ischemia-reperfusion injury in cardiomyocytes via a HIF1alpha-dependent pathway.

11. SENP1 enhances adipogenesis through de-SUMOylation of Sharp-1, which then releases Sharp-1 repression of PPARgamma expression and adipocyte differentiation. These results reveal SENP1 as a novel regulator in adipogenesis.

12. Senp1 Is the Primary Activity for Desumoylation of Sumo1-Modified Proteins.

13. SENP1 is a specific SUMO protease to regulate SUMOylation status of PGC-1alpha.

14. SENP1 is essential for cell survival during endoplasmic reticulum stress.

15. SENP1 is essential for the development of early T and B cells.

16. Data indicates that SENP1 overexpression induces transformation of the normal prostate gland and gradually facilitates the onset of high-grade prostatic intraepithelial neoplasia.

17. SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1.

18. Data describe a mutation in SENP1 that causes increased steady-state levels of the sumoylated forms of a number of proteins and results in placental abnormalities incompatible with embryonic development.

19. These results show that SENP1 plays a key role in the regulation of the hypoxic response through regulation of HIF1alpha stability and that SUMOylation can serve as a direct signal for ubiquitin-dependent degradation.

Xenopus laevis SUMO1/sentrin Specific Peptidase 1 (SENP1) Interaktionspartner

1. XSENP1a and XSENP1b are sumo-specific proteases that inhibit normal head formation by inhibiting Wnt/beta-catenin signaling.