Oligomerization of the microtubule-associated protein tau is mediated by its N-terminal sequences: implications for normal and pathological tau action
H. Eric Feinstein, Sarah J. Benbow, Nichole E. LaPointe, Nirav Patel, Srinivasan Ramachandran, Thanh D. Do, Michelle R. Gaylord, Noelle E. Huskey, Nicolette Dressler, Megan Korff, Brady Quon, Kristi Lazar Cantrell, Michael T. Bowers, Ratnesh Lal and Stuart C. Feinstein
Version of Record online: 20 APR 2016 | DOI: 10.1111/jnc.13604
The microtubule-associated protein tau is essential for neuronal development and maintenance, but is also central to Alzheimer's and related dementias. Unfortunately, the molecular mechanisms underlying normal and pathological tau action remain poorly understood. Here, we demonstrate that tau can homo-oligomerize, providing novel mechanistic models for normal tau action (promoting microtubule growth and bundling, suppressing microtubule shortening) and pathological tau action (poisoning of oligomeric complexes).