TY  - JOUR
AU  - Jansen, Séverine
AU  - Narasimhan, Subhash
AU  - Cabre Fernandez, Paula
AU  - Iľkovičová, Lucia
AU  - Kozeleková, Aneta
AU  - Králová, Kateřina
AU  - Hritz, Jozef
AU  - Žídek, Lukáš
TI  - Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14‐3‐3ζ
JO  - The FEBS journal
VL  - 292
IS  - 8
SN  - 0014-2956
CY  - Oxford [u.a.]
PB  - Wiley-Blackwell
M1  - PUBDB-2025-01461
SP  - 1991 - 2016
PY  - 2025
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:39877981
UR  - <Go to ISI:>//WOS:001408033600001
DO  - DOI:10.1111/febs.17405
UR  - https://bib-pubdb1.desy.de/record/626508
ER  -