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TTLL7, or Tubulin tyrosine ligase-like protein 7, is a member of the tubulin tyrosine ligase-like (TTLL) enzyme family that catalyzes polyglutamylation, a post-translational modification where glutamate chains are added to specific residues on the C-terminal tail of beta-tubulin. TTLL7 is ATP-dependent and capable of both initiating and elongating polyglutamate chains, showing preferential activity on beta-tubulin over alpha-tubulin. This modification regulates microtubule dynamics, affecting neuronal development and cellular transport by modulating microtubule-associated protein interactions. TTLL7 is highly expressed in the nervous system, and its activity is essential for proper growth of MAP2-positive neurites. Mutations or dysregulation of TTLL7 and related TTLL family proteins have been linked to several neurodegenerative diseases, indicating potential disease relevance as a therapeutic target
No specific mechanism for therapeutic inhibition or activation described; mechanistically, polyglutamylases catalyze the ATP-dependent addition of glutamate chains to tubulin
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