9FVL

Dimeric 14-3-3 zeta in complex with unphosphorylated MAP2c peptide

Summary for 9FVL

• Entry DOI: 10.2210/pdb9fvl/pdb
• Related: 9FUM
• Descriptor: 14-3-3 protein zeta/delta, Isoform 3 of Microtubule-associated protein 2, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: regulation, mictorubule dynamics, cytoskeleton, phosphorylation, structural protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 63136.45

Authors

Narasimhan, S.,Jansen, S.,Zidek, L. (deposition date: 2024-06-27, release date: 2025-02-12)

Primary citation

Jansen, S.,Narasimhan, S.,Cabre Fernandez, P.,Ilkovicova, L.,Kozelekova, A.,Kralova, K.,Hritz, J.,Zidek, L.
Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3 zeta.
Febs J., 2025

PubMed Abstract: 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.

PubMed: 39877981
DOI: 10.1111/febs.17405

Experimental method

X-RAY DIFFRACTION (2.08 Å)