Hosted by Les Wilson and Stu Feinstein
2:00pm October 31st
MSRB (Marine Science Research Bldg) Auditorium
Reception on the 2nd Floor Deck Immediately Afterwards
Attire: Costumes preferred
Why do neurons generate multiple isoforms of the microtubule-associated protein tau in a developmentally-coordinated manner? How does disruption of tau isoform balance in neurons cause neurodegenerative disease in humans? In this study, we used a kinesin-driven microtubule gliding assay as a molecular reporter for tau induced changes in intrinsic microtubule surface topography. We find that assembly of microtubules by either 3R or 4R tau differentially regulates gliding velocity, independent of tau concentration. We suggest that these different velocities reflect distinct tau-induced topographies intrinsic to the MT surface. Additionally we find that kinesin dramatically stabilizes microtubule dynamic instability, while both tau isoforms increase microtubule rigidity. Together, these tau-mediated effects upon structure and function may be critical for proper neuronal development and maintenance, and when impaired, could lead to neurodegenerative disease.