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. 2017 May 1;28(9):1271–1283. doi: 10.1091/mbc.E17-01-0008

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© 2017 Ho 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 6: — ART degradation in ubp2Δ ubp15Δ is not mediated by ubiquitination at the activating lysine residues. (A) Protein extracts of art1Δ and art1Δ ubp2Δ ubp15Δ yeast cells expressing plasmid-encoded Art1-FLAG or Art1^K486R-FLAG were analyzed by SDS–PAGE and immunoblot. (B) Protein extracts of art4Δ and art4Δ ubp2Δ ubp15Δ yeast cells expressing plasmid-encoded Art4-FLAG or Art4^{K(235/245/264/267)R}-FLAG were analyzed by SDS–PAGE and immunoblot. (C) Protein extracts of art4Δ and art4Δ ubp2Δ ubp15Δ cells expressing plasmid-encoded Art4-HA or Art4^27KR-HA were analyzed by SDS–PAGE and immunoblot. (D) Relative Art4 levels (art4Δ ubp2Δ ubp15Δ cells vs. art4Δ cells) as in C were quantified using the LI-COR system. Data from three independent experiments are presented as mean ± SD. (E) Model for functionally distinct ubiquitinations of ARTs. Rsp5 ubiquitinates Art1 at K486 and Art4 at K235/K245/K264/K267, which are required for their activation. In the absence of Ubp2 and Ubp15, additional lysines on ARTs are ubiquitinated, causing their degradation.