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. 2011 Aug 1;22(15):2702–2715. doi: 10.1091/mbc.E11-02-0115

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© 2011 Roth 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 9: — A model for how the three Yck2 palmitoylation domains may collaborate to promote Akr1-mediated palmitoylation. The KD and CCTP are hypothesized to interact with two separate Akr1 domains, the ankyrin repeats and the active site DHHC loop, respectively. The poorly conserved CTD, which is predicted to be intrinsically disordered is suggested to be a flexible linker that facilitates the simultaneous interaction of the KD and the CCTP with Akr1.