%0 Journal Article
%A Jansen, Séverine
%A Narasimhan, Subhash
%A Cabre Fernandez, Paula
%A Iľkovičová, Lucia
%A Kozeleková, Aneta
%A Králová, Kateřina
%A Hritz, Jozef
%A Žídek, Lukáš
%T Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14‐3‐3ζ
%J The FEBS journal
%V 292
%N 8
%@ 0014-2956
%C Oxford [u.a.]
%I Wiley-Blackwell
%M PUBDB-2025-01461
%P 1991 - 2016
%D 2025
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:39877981
%U <Go to ISI:>//WOS:001408033600001
%R 10.1111/febs.17405
%U https://bib-pubdb1.desy.de/record/626508