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.

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