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Mass photometry to study the oligomerization of HACE1

RECORD | Already taken place We, 15.5.2024
Together with biophysical analyses including HDX-MS and mass photometry, our studies reveal how HACE1 is regulated and how it recognizes its substrate with specificity.
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Wiley: Mass photometry to study the oligomerization of HACE1
Wiley: Mass photometry to study the oligomerization of HACE1

Protein ubiquitination is a versatile post-translational modification that orchestrates many cellular pathways. Ubiquitin ligases are key specificity factors in this system. The HECT-type ubiquitin ligase HACE1 controls membrane dynamics and redox homeostasis by mechanisms that are still poorly understood at a structural level.

We determined the cryo-EM structures of HACE1 alone and in complex with its physiological substrate, RAC1. Together with biophysical analyses including HDX-MS and mass photometry, our studies reveal how HACE1 is regulated and how it recognizes its substrate with specificity. I am going to provide an overview of this work with a specific focus on the use of mass photometry.

All participants in this webinar will receive a Certificate of Attendance.

Presenter: Sonja Lorenz (Research Group Leader, Max Planck Institute for Multidisciplinary Sciences)

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