Asian investor commits $15M to launch new protein degradation biotech startup Cullgen out of UNC
A Japan-based investor with close ties to Chinese research circles is backing a new biotech upstart in the US with its own take on the hot field of protein degradation.
Tokyo-based GNI Group is providing up to $15 million to seed the work at a newco called Cullgen, the brainchild of UNC investigator Yue Xiong. While still very much a fledgling, the company’s launch plans call for research to be undertaken in the US, Japan as well as China.
Like others in the field, they’ll be focused on ubiquitin-mediated protein degradation technology. Xiong has been working on developing new drugs found through his investigation of enzymes present in the cullin-RING family of E3 ubiquitin ligases. And the company will set off with some targets in oncology and then spread out to inflammation and autoimmune disease.
It’s a thriving field.
Genentech and Pfizer inked recent deals with Arvinas, which is building on the lab work of Yale’s Craig Crews on protein degradation. Atlas backed Kymera’s launch last fall. And NIBR chief and protein degradation expert Jay Bradner, who earlier founded C4 to delve into this, forged an alliance with UC Berkeley that will dive deep into protein degradation.
Cullgen represents the arrival of new Asian investors in the US, the global R&D structure that’s being developed to support startups as well as the overall funding frenzy that has focused closely on cancer R&D over the past two years.
So what will Cullgen go after? Xiong’s home page on the UNC website includes this segment on protein degradation:
Most, if not all, cellular processes, including notably cell cycle control and p53 control, are regulated by ubiquitin-mediated modification and degradation. The mechanisms targeting specific proteins for ubiquitylation, in most cases, are poorly understood. We discovered two novel RING finger proteins, ROC1 and ROC2, which constitute active ubiquitin ligases with members of the cullin family. We also discovered that Cullins 3 and 4 could assemble in vivo as many as 200 and 100 distinct E3 ubiquitin ligases, respectively. Our current research in this area is focused on two issues. (1) Developing a strategy to systematically identify the substrates of the cullin-RING E3 ligases, and (2) Elucidating the mechanism of CUL4 E3 ligases in control of gene expression and chromatin structure.
Lisa Carey, Stephen Frye and Peter Jackson are joining the SAB while Ying Luo, the CEO of GNIG, Yue Xiong, Jian Jin, and GNIG CFO Thomas Eastling will sit on the board.