國家衛生研究院 NHRI:Item 3990099045/7643
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    题名: Caveolin-1 interacts with derlin-1 and promotes ubiquitination and degradation of cyclooxygenase-2 via collaboration with p97 complex
    作者: Chen, SF;Wu, CH;Lee, YM;Tam, K;Tsai, YC;Liou, JY;Shyue, SK
    贡献者: Institute of Cellular and Systems Medicine
    摘要: Caveolin-1 (Cav-1) interacts with and mediates protein trafficking and various cellular functions. Derlin-1 is a candidate for the retrotranslocation channel of endoplasmic reticulum proteins. However, little is known about how Derlin-1 mediates glycosylated protein degradation. Here, we identified Cav-1 as a key player in Derlin-1- and p97-mediated cyclooxygenase 2 (COX-2) ubiquitination and degradation. Derlin-1 augmented the interaction of Cav-1 and COX-2 and mediated the degradation of COX-2 in a COX-2 C terminus-dependent manner. Suppression of Cav-1 decreased the ubiquitination of COX-2, and mutation of Asn-594 to Ala to disrupt N-glycosylation at the C terminus of COX-2 reduced the interaction of COX-2 with Cav-1 but not Derlin-1. Moreover, suppression of p97 increased the ubiquitination of COX-2 and up-regulated COX-2 but not COX-1. Cav-1 enhanced the interaction of p97 with Ufd1 and Derlin-1 and collaborated with p97 to interact with COX-2. Cav-1 may be a cofactor in the interaction of Derlin-1 and N-glycosylated COX-2 and may facilitate Derlin-1- and p97 complex- mediated COX-2 ubiquitination, retrotranslocation, and degradation.
    日期: 2013-11-15
    關聯: Journal of Biological Chemistry. 2013 Nov 15;288(46):33462-33469.
    Link to: http://dx.doi.org/10.1074/jbc.M113.521799
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=1083-351X&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000328841700058
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84887831038
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