1. The present study demonstrated for the first time that knockdown of Hakai inhibited the proliferation, migration and invasion of nonsmallcell lung cancer cells, and sensitized nonsmallcell lung cancer cells to cisplatin. PMID: 29786107
2. findings suggest that the E3 ubiquitin-ligase, such as Hakai, may be a better target than proteasome for using novel specific inhibitors in tumor subtypes that follow EMT. PMID: 28675930
3. These results suggest that stabilization of delta-catenin by Hakai is dependent on Src. PMID: 28069439
4. these observations suggest that the dimeric architecture of the HYB domain is essential for the phosphotyrosine-binding property of Hakai. PMID: 25074933
5. By lowering Hakai abundance, miR-203 also reduces Hakai-regulated-cell division. PMID: 23285092
6. Hakai dimerization allows the formation of a phosphotyrosine-binding pocket that recognizes specific phosphorylated tyrosines and flanking acidic amino acids of Src substrates, such as E-cadherin, cortactin and DOK1. PMID: 22252131
7. Hakai mediates E-cadherin ubiquitination and degradation triggered by Slit-Robo signaling during colorectal epithelial cell carcinogenesis. PMID: 21283129
8. Together, these data do not support a requirement for CBLL1 during flavivirus entry and rather suggest an essential role of the ubiquitin/proteasome pathway for flavivirus genome amplification. PMID: 21191016
9. Results suggest that Hakai is a novel corepressor of ERalpha and may play a negative role in the development and progression of breast cancers. PMID: 20608937
10. Results suggest that Hakai is an important regulator of cell proliferation and that Hakai may be an oncoprotein and a potential molecular target for cancer treatment. PMID: 19535458

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HGNC: 21225

OMIM: 606872

KEGG: hsa:79872

STRING: 9606.ENSP00000401277

UniGene: Hs.592271