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. 2015 Jul 1;26(13):2426–2438. doi: 10.1091/mbc.E14-10-1462

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© 2015 Yamashita et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 5: — Lgl2-VprBP-DDB1 complex was well formed with reduction of CRL4 [VprBP] complex in confluent cells. (A) Lgl2 was immunoprecipitated from the lysates of MDCK cells cultured in confluent or low-density conditions. The amount of coprecipitated VprBP was higher from confluent cells. (B) VprBP was immunoprecipitated from MDCK cell lysates cultured in confluent or low-density conditions. The amount of coprecipitated Cul4A was lower from confluent cells. (C) Hypothetical model of Lgl-mediated inhibition of the CRL4 [VprBP] complex and its downstream pathway. Lgl forms a complex with VprBP-DDB1 independently of Cul4A when cells reach confluency. Lgl-VprBP-DDB1 complex is catalytically inactive because it lacks Cul4A and Roc1, the active center that associates with E2 enzyme.