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. 2013 Sep 15;24(18):2990–2999. doi: 10.1091/mbc.E13-04-0204

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© 2013 Shin 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 7: — A proposed model for the role of PAK1^S223 phosphorylation in PAK1 activation. PAK1 activation involves conformational changes that lead to the conversion of an inactive dimeric PAK1 to an active monomeric form. This conversion, however, is not sufficient to bring about PAK1 activation; it is required for PAK1 phosphorylation at S223 by CK2. This phosphorylation is thought to lock the PAK1 kinase domain in a catalytically competent form. S223 phosphorylation does not directly affect phosphorylation of T423; however, the possibility is not excluded that CK2 might activate PDK1 by activating the PI3K/Akt signaling via PTEN and positively regulate T423 phosphorylation.