anti-Speckle-Type POZ Protein (SPOP-B) 抗体

Human Speckle-Type POZ Protein (SPOP-B) interaction partners

1. An SPOP interactome analysis shows that wild type (WT) SPOP but not mutant SPOP associates with multiple proteins involved in transcription, mRNA splicing and export.

2. no evidence that ERG is an effector of SPOP mutation in human prostate cancer or mouse models.

3. LINC01638 interacts with c-Myc to prevent SPOP-mediated c-Myc ubiquitination.

4. Disease-associated SPOP mutations that lead to the accumulation of proto-oncogenic proteins interfere with phase separation and co-localization in membraneless organelles, suggesting that substrate-directed phase separation of this E3 ligase underlies the regulation of ubiquitin-dependent proteostasis

5. SPOP inhibits NF-kappaB (nuclear factor kappa-light-chain-enhancer of activated B cells) activity and its target genes expression via FADD in non-small cell lung cancer

6. TRIM24 and AR coactivated gene signature of SPOP-mutant prostate cancer (PCa) is similarly activated in human PCa with high TRIM28 expression.

7. SPOP inhibits hepatocellular carcinoma (HCC) cell metastasis via ubiquitin-dependent SENP7 proteolysis and may thus serve as a new opinion for the prevention of HCC metastasis.

8. Our result suggests that SPOP expression in blood might have a sensitivity that is low for routine diagnostic use and for screening for Renal cell carcinoma (RCC). However, SPOP could be a potential tissue diagnostic biomarker in RCC.

9. Expression of the F133V mutation and wild-type SPOP was at much lower levels compared to that of F102C and Y87N mutations; however, at present, it is unknown if this also affects the biological activity of the SPOP protein.

10. PD-L1 protein abundance is regulated by cyclin D-CDK4 and the cullin 3-SPOP E3 ligase via proteasome-mediated degradation

11. methylation status of SPOP promoter can be used as a novel epigenetic biomarker and a therapeutic target in colorectal cancer.

12. these data highlight SPOP as an important regulator of luminal epithelial cell proliferation and c-MYC expression in prostate physiology, identify c-MYC as a novel bona fide SPOP substrate, and help explain the frequent inactivation of SPOP in human prostate adenocarcinoma.

13. Results elucidate the tumor-suppressor role of SPOP in prostate cancer in which it acts as a negative regulator of BET protein stability and also provide a molecular mechanism for resistance to BET inhibitors in individuals with prostate cancer bearing SPOP mutations.

14. SPOP mutation in endometrial cancer increased degradation of BRD2, BRD3 and BRD4 proteins. SPOP mutation in prostate cancer increased expression of BRD2, BRD3 and BRD4 proteins.

15. Prostate cancer-derived SPOP mutants failed to interact with Cdc20 to promote its degradation. As a result, SPOP-deficient prostate cancer cells with elevated Cdc20 expression became resistant to a pharmacological Cdc20 inhibitor.

16. While wild-type SPOP localizes to liquid nuclear speckles, self-association-deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains.

17. SPOP mutation activates both PI3K/mTOR and androgen receptor signaling, effectively uncoupling the normal negative feedback between these two pathways.

18. SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing.

19. The levels of SPOP significantly decreased, while the levels of SIRT2 significantly increased in non-small cell lung cancer (NSCLC) cell lines, compared to normal bronchial epithelial cell line and NSCLC specimens, compared to the paired non-tumor lung tissue.

20. hese findings reveal novel molecular events underlying the regulation of INF2 function and localization, and provided insights in understanding the relationship between SPOP mutations and dysregulation of mitochondrial dynamics in prostate cancer.

Mouse (Murine) Speckle-Type POZ Protein (SPOP-B) interaction partners

1. no evidence that ERG is an effector of SPOP mutation in human prostate cancer or mouse models.

2. loss of Spop, but not Spopl, disrupts chondrocyte hypertrophy and osteoblast differentiation in the mouse, suggesting the requirement for Spop-mediated protein degradation in mouse skeletal development; overexpressed Spop targets both Gli3FL and Gli3R for ubiquitination and degradation and Spop is an important positive regulator of Ihh signaling and skeletal development

3. Results demonstrate a negative role of Spop in the level and activity of Gli3, Shh signaling and ventral spinal cord patterning.

4. Speckle-type pox virus and zinc finger (POZ) protein (SPOP) regulates endometrial stromal cell decidualization in mice and that hormones regulate the expression of SPOP. This study suggests that ubiquitination may be involved in embryonic implantation.

5. These results implicate SPOP as a novel participant in DNA double strand break repair and suggest that SPOP mutation drives prostate tumorigenesis in part through genomic instability.

6. miR-145 has a role in post-transcriptional regulation of SPOP expression in selected tissues.

7. Dzip1-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli/Ci proteins in the Hh pathway.

8. similar S/T-rich motifs are present in Gli proteins as well as in numerous HIB-interacting proteins and mediate Gli degradation by SPOP

9. MacroH2A1.2 binds the nuclear protein Spop.

10. Interaction of endogenous PDX-1 and PCIF1 in MIN6 insulinoma cells, is demonstarted.

Xenopus laevis Speckle-Type POZ Protein (SPOP-B) interaction partners

1. Dzip1-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli/Ci proteins in the Hh pathway.