Madelon Maurice is appointed Full Professor at the UMC Utrecht and member of the national Oncode Institute for cancer research. She is internationally recognized for contributing key mechanistic insights into how stem cell-niche communication controls tissue renewal, and how cancer mutations impact on these processes. Her academic group employs a multiscale approach that allows for the investigation of molecular processes in complex tissues using organoid-based model systems (https://madelonmauricelab.nl/). A longstanding interest is to understand ubiquitinmediated regulation of key signaling pathways, highlighted by i) the discovery that the membrane-bound E3 ligase RNF43 controls Wnt receptor turnover in stem cells, and ii) the
invention of SureTACs technology for targeted membrane protein degradation. The innovative nature of her work was recognized with various prestigious grants (e.g. ERC-St, NWO-VICI, ZonMW-TOP, national Gravitation grant IMAGINE!). She is a regular invited speaker and organizer of international meetings (e.g. GRC, EMBO), is a member of the Oncode research management committee and has co-founded the Utrecht Platform for Organoid Technology. In 2021, Madelon teamed up with seed investor ArgoBio and Oncode to launch the biotech company Laigo Bio. At Laigo Bio,  heterobispecific antibodies (SureTACs) are employed for proximity-induced degradation of membrane-bound proteins.
Madelon is co-founder, shareholder, and chair of the Scientific Advisory Board (SAB) of Laigo Bio.

Membrane-associated proteins are key drivers of cancer, ageing-related diseases and autoimmune disorders and a general strategy to selectively degrade (instead of blocking) these proteins has the potential to improve human health, by o<ering deeper pathway inhibition, tissue-selective targeting
and targeting currently undruggable classes of proteins. Here, we present a novel technology that utilizes cellular endo-lysosomal degrader machinery to target membrane-associated proteins for degradation. To achieve this, we employ heterobifunctional molecules (SureTACs – surface removal
targeting chimeras) that mediate induced proximity of a membrane-bound target and a transmembrane E3 ubiquitin ligase. Upon tethering the E3 to the target, the target protein undergoes ubiquitination, endocytosis and lysosomal degradation.
I will discuss the screening platform that we developed for identification of optimal membranebound E3-target combinations for cell surface removal and degradation of transmembrane proteins. I will share proof-of-principle results of SureTACs that engage a highly potent E3 ligase to
deplete the membrane target protein PD-L1 from the cancer cell surface in an endogenous setting and in vivo in animal models. In ongoing work, we are generating SureTACs that engage di<erent E3 ligases for targeting a variety of membrane proteins, including hard-to-drug targets, thus opening
up new avenues of drug development.