Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3ζ
| Authors | |
|---|---|
| Year of publication | 2025 |
| Type | Article in Periodical |
| Magazine / Source | The FEBS Journal |
| MU Faculty or unit | |
| Citation | |
| web | https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.17405 |
| Doi | http://dx.doi.org/10.1111/febs.17405 |
| Keywords | 14-3-3 proteins; extracellular signal-regulated kinase 2; microtubule-associatedprotein; nuclear magnetic resonance; proteinkinase A |
| Attached files | |
| Description | Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3? 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 14-3-3? with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3? in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3? via its microtubule binding domain and variable central domain. Monomerization of 14-3-3? 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 14-3-3? 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 14-3-3?. |
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