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Figure 5 | BMC Biochemistry

Figure 5

From: Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-Like kinase Mst3

Figure 5

Characterization of Mst3 association with striatin. (A) Three days after transfection with HA-tagged wild-type and mutant striatins, HEK293 cells were lysed and HA-striatin immune complexes were isolated, separated by SDS-PAGE, and immunoblotted. Representative immunoblots are shown. Left, Mst3 binding, like PP2A C subunit binding, requires N-terminal sequences of striatin. Right, unlike PP2A C subunit, Mst3 binding does not require the striatin coiled-coil domain or striatin oligomerization. (B) A similar experiment to (A) was conducted to compare the abilities of Mst3 and Mob3 to bind wild-type striatin and a set of internal striatin deletion mutants localized to regions of unknown function. (C) Relative binding of wild-type and mutant striatins to Mst3 and Mob3 was measured as described in the legend to Figure 2B. The error bars represent the standard deviation of at least three independent experiments. *, p ≤ 0.05; **, p ≤ 0.01 relative to wild-type.

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BMC Biochemistry

ISSN: 1471-2091

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