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Phosphorylation on threonine 11 of ?-dystrobrevin alters its interaction with kinesin heavy chain. (Articolo in rivista)

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Phosphorylation on threonine 11 of ?-dystrobrevin alters its interaction with kinesin heavy chain. (Articolo in rivista) (literal)

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Fratini F, Macchia G, Torreri P, Matteucci A, Salzano AM, Crescenzi M, Macioce P, Petrucci TC, Ceccarini M. (2012)
Phosphorylation on threonine 11 of ?-dystrobrevin alters its interaction with kinesin heavy chain.
in FEBS journal. S (Online); Wiley-Blackwell, Oxford (Regno Unito)
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Fratini F, Macchia G, Torreri P, Matteucci A, Salzano AM, Crescenzi M, Macioce P, Petrucci TC, Ceccarini M. (literal)

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Department of Cell Biology and Neuroscience, Istituto Superiore di Sanità, Rome, Italy Department of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità, Rome, Italy National Centre for Rare Diseases, Istituto Superiore di Sanità, Rome, Italy Proteomics & Mass Spectrometry Laboratory, ISPAAM, National Research Council, Naples, Italy (literal)

Titolo

Phosphorylation on threonine 11 of ?-dystrobrevin alters its interaction with kinesin heavy chain. (literal)

Abstract

Dystrobrevin family members (? and ?) are cytoplasmic components of the dystrophin-associated glycoprotein complex, a multimeric protein complex first isolated from skeletal muscle, which links the extracellular matrix to the actin cytoskeleton. Dystrobrevin shares high homology with the cysteine-rich and C-terminal domains of dystrophin and a common domain organization. The ?-dystrobrevin isoform is restricted to nonmuscle tissues, serves as a scaffold for signaling complexes, and may participate in intracellular transport through its interaction with kinesin heavy chain. We have previously characterized the molecular determinants affecting the ?-dystrobrevin-kinesin heavy chain interaction, among which is cAMP-dependent protein kinase [protein kinase A (PKA)] phosphorylation of ?-dystrobrevin. In this study, we have identified ?-dystrobrevin residues phosphorylated in vitro by PKA with pull-down assays, surface plasmon resonance measurements, and MS analysis. Among the identified phosphorylated residues, we demonstrated, by site-directed mutagenesis, that Thr11 is the regulatory site for the ?-dystrobrevin-kinesin interaction. As dystrobrevin may function as a signaling scaffold for kinases/phosphatases, we also investigated whether ?-dystrobrevin is phosphorylated in vitro by kinases other than PKA. Thr11 was phosphorylated by protein kinase C, suggesting that this represents a key residue modified by the activation of different signaling pathways. (literal)

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