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• W2022191921 startingPage "130" @default.
• W2022191921 abstract "Cytokine-inducible SH2-containing protein (CIS) inhibits prolactin receptor (PRLR) signaling and acts as part of an E3 ubiquitin ligase complex through interactions with Elongin B/C proteins. This study aimed to identify CIS lysine ubiquitination sites and determine roles of ubiquitination and Elongin B/C interactions on CIS protein stability and PRLR signaling inhibition. Site-directed mutations revealed that CIS can be ubiquitinated on all six lysine residues. Elongin B/C interaction box mutation had no influence on CIS ubiquitination. CIS stability was increased by mutation of lysine residues and further enhanced by co-mutation of Elongin B/C interaction domain. CIS inhibition of STAT5B phosphorylation and casein promoter activation was dependent on CIS interactions with Elongin B/C, but not on CIS ubiquitination. These data indicate CIS protein stability is regulated through multiple mechanisms, including ubiquitination and interaction with Elongin B/C proteins, whereas CIS functional inhibition of PRLR signaling is dependent on the Elongin B/C interaction." @default.
• W2022191921 created "2016-06-24" @default.
• W2022191921 creator A5043565774 @default.
• W2022191921 creator A5052009072 @default.
• W2022191921 date "2015-02-01" @default.
• W2022191921 modified "2023-10-16" @default.
• W2022191921 title "Regulation of cytokine-inducible SH2-containing protein (CIS) by ubiquitination and Elongin B/C interaction" @default.
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• W2022191921 doi "https://doi.org/10.1016/j.mce.2014.10.017" @default.
• W2022191921 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4373541" @default.
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