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. 2017 Sep 1;2017:6210694. doi: 10.1155/2017/6210694

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Copyright © 2017 Ke Mao et al.

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Sal A promotes P62-CYLD-TRAF6 interaction. (a) ARPE-19 cells were classified and treated as before. Coimmunoprecipitation assay was to determine P62-CYLD-TRAF6 interaction 48 hours after Sal A and/or OX-LDL stimulation. (a) TRAF6 was isolated by IP followed by detection of the associated CYLD by IB. The cell lysates were subjected to IB to monitor the expression of CYLD and TRAF6. (b)TRAF6 was isolated by IP, and its ubiquitination form was detected by IB. (c) Endogenous CYLD was isolated by IP followed by IB to detect the associated P62. P62 and CYLD protein expressions in cell lysates were monitored by direct IB. Compared to the OX-LDL group, the OX-LDL + Sal A group induced P62-CYLD TRAF6 interaction and promoted deubiquitination of TRAF6.