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U.S.A."],"published-print":{"date-parts":[[2015,6,16]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>Tau is an important microtubule-associated protein. Although the structure\u2013function relationship of Tau has been intensively studied for many years primarily by molecular biology and biochemical approaches, little is still known about the molecular mechanisms by which Tau interacts with microtubules and promotes microtubule assembly. Here, we provide detailed insight into the Tau\u2013microtubule association by using NMR spectroscopy and mass spectrometry. We show that Tau binds to microtubules by using small groups of residues, which are important for pathological aggregation of Tau. We further show that Tau stabilizes a straight protofilament conformation by binding to a hydrophobic pocket in between tubulin heterodimers. 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