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Ronald A. Merrill, Andrew M. Slupe and Stefan Strack N-terminal phosphorylation of protein phosphatase 2A/Bβ2 regulates translocation to mitochondria, dynamin-related protein 1 dephosphorylation, and neuronal survival The FEBS Journal 280

Version of Record online: 8 JUN 2012 | DOI: 10.1111/j.1742-4658.2012.08631.x

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Bβ2, a neuron-specific regulatory subunit of PP2A, is regulated by phosphorylation of serines in the N–terminal mitochondrial targeting sequence. Blocking phosphorylation (SerAla mutation) promotes outer-mitochondrial localization of PP2A/Bβ2, activation of the mitochondrial fission enzyme Drp1 by dephosphorylation, and neuronal death. Conversely, phosphomimetic substitution of Bβ2 (SerAsp) has opposite effects. Thus, reversible phosphorylation regulates the mitochondrial fission/fusion equilibrium at multiple levels.

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