IndraLab

"S60 of CSN6 is phosphorylated by PKB/Akt [ xref ] and is critical for CSN6 stabilization."

"CSN6 S60 phosphorylation is known to increase the stability of CSN6 [21]."

"First, we have shown that S60 of CSN6 can be phosphorylated by PKB/Akt [ xref ] and that PKB/Akt enhances the steady‐state expression of CSN6. [ xref ] This S60 site is located in CSN6's MPN ( M pr1p and P ad1p N ‐terminal) domain, a domain found in the N‐terminus of yeast Mpr1 and Pad1 proteins. [ xref , xref , xref ] MPN domain contains polar residues that resemble the active site residues of metalloproteases [ xref ] and is involved in a proteasome‐associated deneddylation activity. [ xref ] Also the MPN domain is involved in heterodimerization between CSN6 and CSN5 to regulate Cullin neddylation. [ xref ] How S60 phosphorylation participates in any activity of the MPN domain remains to be identified."

"CSN6 S60 phosphorylation is known to increase the stability of CSN6 [ xref ]."

"Our mechanistic studies showed that EGF/Akt-mediated CSN6 S60 phosphorylation and subse quent stabilization of E6AP thereby causing p53 downregulation and promoting cell proliferation, cell transformation as well as tumorigenesis (Figure xref )."

"Our mechanistic studies showed that EGF/Akt-mediated CSN6 S60 phosphorylation and subse quent stabilization of E6AP thereby causing p53 downregulation and promoting cell proliferation, cell transformation as well as tumorigenesis (Figure 8)."

"Akt is able to associate with CSN6 and phosphorylate it at Ser60, which can reduce the ubiquitin-mediated protein degradation and turnover rate of CSN6, thereby increasing steady-state expression of CSN6."