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100 1 _ |a Jansen, Séverine
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245 _ _ |a Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14‐3‐3ζ
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520 _ _ |a Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3ζ in a cAMP-dependent protein kinase (PKA) phosphorylation dependent manner. Using selective phosphorylation, calorimetry, nuclear magnetic resonance, chemical crosslinking, and X-ray crystallography, we characterized interactions of 14-3-3ζ with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3ζ in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3ζ via its microtubule binding domain and variable central domain. Monomerization of 14-3-3ζ leads to the loss of affinity for the unphosphorylated residues. In neuroblastoma cell extract, MAP2c is heavily phosphorylated by PKA and the proline kinase ERK2. Although 14-3-3ζ dimer or monomer do not interact with the residues phosphorylated by ERK2, ERK2 phosphorylation of MAP2c in the C-terminal domain reduces the binding of MAP2c to both oligomeric variants of 14-3-3ζ.
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700 1 _ |a Narasimhan, Subhash
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700 1 _ |a Cabre Fernandez, Paula
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700 1 _ |a Iľkovičová, Lucia
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700 1 _ |a Kozeleková, Aneta
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700 1 _ |a Králová, Kateřina
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700 1 _ |a Hritz, Jozef
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700 1 _ |a Žídek, Lukáš
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773 _ _ |a 10.1111/febs.17405
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