Dataset Information

LC-MS data of IM95 gastric cancer cells following YAP degradation by bioPROTAC

ABSTRACT: In this study, through naïve nanobody phage library screening, we have identified multiple nanobodies against human YAP with high affinity and specificity. The YAP nanobody was then fused to the RING domain of RNF4, creating a bio-Proteolysis-Targeting Chimera (bioPROTAC) molecule capable of selectively targeting endogenous YAP for ubiquitin-mediated degradation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Regulation Of Gastric Acid Secretion, Cell Culture

DISEASE(S): Diffuse Gastric Cancer

SUBMITTER: Gui-Ming Zhang

LAB HEAD: Gui-Ming Zhang

PROVIDER: PXD063726 | Pride | 2025-11-03

REPOSITORIES: Pride

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Targeted degradation of endogenous YAP by nanobody bioPROTAC inhibits tumor progression.

Zhou Runhua R Wang Huifang H Zhang Gui-Ming GM Liu Yawei Y Liu Xiao-Lian XL Li Zhifen Z Shi Guangwei G Yuan Junling J Qu Chengming C Li Yang Y Chen Liang L Huang Jingnan J Zhou Hongchao H Dai Lingyun L Bai Chongzhi C Wang Jigang J Yu Le L Li Zhijie Z Li Yi-Lei YL

Nature communications 20251023 1

Yes-associated protein (YAP), a key effector of the Hippo pathway, regulates gene expression and promotes tumorigenesis. YAP is conventionally considered "undruggable", however, targeted protein degradation offers a promising approach to address the challenges associated with targeting this oncogenic protein. In this study, through naïve nanobody phage library screening, we identify multiple nanobodies against human YAP with high affinity and specificity. The YAP nanobody is then fused to the RI ...[more]

PMID: 41130953

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