Disrupting VDAC1–tubulin interaction uncovers crosstalk between mitochondrial and microtubule functions with implication to cancer therapy

Tubulin, a key component of the microtubule (MT) cytoskeleton, interacts with the mitochondrial gatekeeper protein VDAC1. Using a peptide array, we identified four VDAC1-binding sites in α-tubulin-1B. Synthetic peptides corresponding to these sequences bound purified VDAC1, disrupted MT polymerization and structure, and impaired MT function. In cells, the peptides disrupted the MT network, reduced tubulin and glucose transporter (Glut-1) expression, induced p53 and VDAC1 overexpression, triggere