Korchak Emilie J, Sharafi Mona, Maisonet Isabella Jaen, Caro Pilar, Schaaf Christian P, Buhrlage Sara J, Bezsonova Irina
Department of Molecular Biology and Biophysics, UCONN Health, Farmington, Connecticut 06032, United States.
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, United States.
bioRxiv. 2025 Mar 20:2025.03.20.644318. doi: 10.1101/2025.03.20.644318.
Hao-Fountain syndrome is a rare neurodevelopmental disorder caused by mutations in the de-ubiquitinating enzyme USP7 (Ubiquitin Specific Protease 7). Due to the novelty of the disease and its poorly understood molecular mechanisms, treatments for the syndrome are currently lacking. This study examines the effects of 11 patient-derived variants located within the catalytic domain of USP7, focusing on their impact on the enzyme's activity, thermodynamic stability, and substrate recognition. Our findings reveal a spectrum of functional consequences, ranging from complete inactivation to hyperactivation of USP7. Notably, we identify a specific subset of pathogenic variants whose catalytic activity can be significantly boosted using a novel allosteric activator. These results provide the first insight into USP7 malfunction in Hao-Fountain syndrome-linked variants and pave the way for improved prognostic approaches and targeted treatments in the future.
郝 - 方丹综合征是一种罕见的神经发育障碍,由去泛素化酶USP7(泛素特异性蛋白酶7)的突变引起。由于该疾病的新颖性及其分子机制尚不清楚,目前缺乏针对该综合征的治疗方法。本研究考察了位于USP7催化结构域内的11个患者来源变体的影响,重点关注它们对酶活性、热力学稳定性和底物识别的影响。我们的研究结果揭示了一系列功能后果,从USP7的完全失活到超激活。值得注意的是,我们鉴定出了一个特定的致病变体子集,其催化活性可以使用一种新型变构激活剂得到显著增强。这些结果首次深入了解了郝 - 方丹综合征相关变体中USP7的功能障碍,并为未来改进预后方法和靶向治疗铺平了道路。