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. 2012 Apr 15;23(8):1475–1485. doi: 10.1091/mbc.E11-11-0957

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© 2012 Frijns 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 8. — Model for phosphorylation-induced dissociation of the β4-plectin complex. Phosphorylation of β4 on T1736 by PKD1 or other CAMK-like kinases results in the dissociation of the C-tail and the plakin domain of plectin, whereas phosphorylation of β4 at S1356 and S1364 by ERK1/2 and p90RSK1/2 causes a loss of plectin-ABD binding. Subsequent binding of plectin to F-actin or Ca²⁺/calmodulin may shift the equilibrium toward complete disassociation of the β4-plectin complex.