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Federica Fratini, Gianfranco Macchia, Paola Torreri, Andrea Matteucci, Anna Maria Salzano, Marco Crescenzi, Pompeo Macioce, Tamara C. Petrucci and Marina Ceccarini Phosphorylation on threonine 11 of β-dystrobrevin alters its interaction with kinesin heavy chain The FEBS Journal 279

Version of Record online: 11 OCT 2012 | DOI: 10.1111/febs.12006

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β-dystrobrevin, a component of the dystrophin complex, can be phosphorylated by PKA and PKC. By mass spectrometry analysis, we have identified β-dystrobrevin residues phosphorylated in vitro by both the kinases and, using pull-down assays and surface plasmon resonance measurements, demonstrated that threonine 11 is a key residue for β-dystrobrevin–kinesin interaction.

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