Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3ζ
| Autoři | |
|---|---|
| Rok publikování | 2025 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | FEBS Journal |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | https://www.scopus.com/record/display.uri?eid=2-s2.0-85216564822&origin=resultslist&sort=plf-f&src=s&sot=b&sdt=b&s=DOI%2810.1111%2Ffebs.17405%29&sessionSearchId=f3ef5b6b47cafc6f00903901da30253e |
| Doi | http://dx.doi.org/10.1111/febs.17405 |
| Klíčová slova | 14-3-3 proteins; extracellular signal-regulated kinase 2; microtubule-associated protein; nuclear magnetic resonance; protein kinase A |
| Popis | Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3 zeta 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 zeta with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3 zeta in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3 zeta via its microtubule binding domain and variable central domain. Monomerization of 14-3-3 zeta 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 zeta 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 zeta. |
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