University of Cambridge > Talks.cam > Biophysical Seminars > Controlling Protein Damage

Controlling Protein Damage

Add to your list(s) Download to your calendar using vCal

If you have a question about this talk, please contact Jerome Charmet.

All welcome

Molecular chaperones such as the Hsp90 chaperone are the first line of the cellular defense system against protein damage and aggregation. The chaperones are part of the proteostasis network, the natural defense system against protein damage problems. Hsp90 interacts in vivo and in vitro with the Tau protein, the molecular basis of this interaction remained enigmatic. We disclosed a structural model of the Hsp90-Tau complex, showing the Tau protein behaves as a bona fide client of the Hsp90 chaperone. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. Our model resolves the paradox on how Hsp90 specifically selects for late folding intermediates but also intrinsically disordered proteins such as Tau. Our data offer a mechanistic understanding how molecular chaperones can deal with aggregates in neurodegenerative diseases.

This talk is part of the Biophysical Seminars series.

Tell a friend about this talk:

This talk is included in these lists:

Note that ex-directory lists are not shown.

 

© 2006-2019 Talks.cam, University of Cambridge. Contact Us | Help and Documentation | Privacy and Publicity