Discovering How 14-3-3ζ Protein Binds to MAP2c

Ever wondered how proteins interact in our cells? Let's dive into the relationship between MAP2c and 14-3-3ζ. MAP2c, a protein that hangs out near microtubules, gets cozy with 14-3-3ζ in a special way. This meeting depends on a process called PKA phosphorylation. Scientists used various tools like calorimetry and X-ray crystallography to figure out how these proteins stick together.

When MAP2c is phosphorylated by PKA, it likes to hug 14-3-3ζ in certain spots, like the proline-rich region and the C-terminal domain. But even when MAP2c isn't phosphorylated, it still finds 14-3-3ζ attractive through its microtubule binding domain and a variable central domain. However, when 14-3-3ζ is alone (monomeric), it doesn't like the unphosphorylated MAP2c as much. In cells from neuroblastoma, MAP2c gets decorated with phosphates by PKA and another protein called ERK2. While 14-3-3ζ isn't into the spots ERK2 phosphorylates, ERK2's phosphorylation in the C-terminal domain makes MAP2c less interested in both forms of 14-3-3ζ.

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