State Key Laboratory of Medical Proteomics, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 100850, China.
Int J Mol Sci. 2024 Aug 15;25(16):8870. doi: 10.3390/ijms25168870.
Bone homeostasis relies on the delicate balance between osteoblast-mediated bone formation and osteoclast-mediated bone resorption. The casein kinase 2 interacting protein-1 (CKIP-1), a specific CK2α subunit-interacting protein, has been documented as one of the crucial negative regulators of bone formation. CKIP-1 siRNA therapy has constraints that limit its use in clinical applications. Therefore, it is necessary to explore effective targeting strategies for CKIP-1. In this study, we observed an upregulation of CKIP-1 protein expression in the microgravity environment, while its ubiquitination levels decreased. We further investigated the interaction between CKIP-1 and VHL and found that VHL enhanced CKIP-1 degradation through the ubiquitylation-proteasome system (UPS). Additionally, we discovered a small molecule ligand, named C77, through DNA-encoded library (DEL) screening, which binds to CKIP-1 both in vivo and in vitro, as confirmed by Surface Plasmon Resonance (SPR) and the Cellular Thermal shift assay (CETSA), respectively. Our findings demonstrated the potential of VHL and C77 as guiding factors in the development of CKIP-1-based Proteolysis-Targeting Chimeras (PROTACs), which could be future therapeutic interventions in disuse osteoporosis.
骨稳态依赖于成骨细胞介导的骨形成和破骨细胞介导的骨吸收之间的微妙平衡。酪蛋白激酶 2 相互作用蛋白-1(CKIP-1)是 CK2α 亚基相互作用蛋白之一,已被证明是骨形成的关键负调控因子之一。CKIP-1 siRNA 治疗存在限制,限制了其在临床应用中的使用。因此,有必要探索 CKIP-1 的有效靶向策略。在这项研究中,我们观察到 CKIP-1 蛋白表达在微重力环境中上调,而其泛素化水平降低。我们进一步研究了 CKIP-1 与 VHL 之间的相互作用,发现 VHL 通过泛素蛋白酶体系统(UPS)增强 CKIP-1 的降解。此外,我们通过 DNA 编码文库(DEL)筛选发现了一种小分子配体,命名为 C77,它在体内和体外都与 CKIP-1 结合,这分别通过表面等离子体共振(SPR)和细胞热转移测定(CETSA)得到证实。我们的研究结果表明,VHL 和 C77 作为基于 CKIP-1 的蛋白水解靶向嵌合体(PROTAC)开发的指导因素具有潜力,这可能是未来治疗废用性骨质疏松症的干预措施。