Microtubule posttranslational modifications provide unique recognition patterns for associated proteins.

Microtubule posttranslational modifications differentially attract or repel specific microtubule-associated proteins, supporting the tubulin code hypothesis.

• Why it matters: Understanding how microtubules interact with associated proteins is crucial for deciphering cellular functions and signaling pathways. The tubulin code suggests PTMs could regulate these interactions, but direct evidence has been limited.
• What they did: Researchers screened 46 proteins for their binding preferences to microtubules with different PTMs or isotype compositions using a medium-throughput in vitro approach.
• The result: They found that subsets of MAPs have unique sensitivities to PTMs, confirming that PTMs can selectively regulate MAP-microtubule interactions, thus providing mechanistic proof for the tubulin code concept.