Supplementary Figure S1-6 from PTEN Loss Promotes PI3Kβ Phosphorylation and EPHA2/SRC/p-PI3KβY962 Complex Assembly to Drive Tumorigenesis
Year: 2026
Type: supplementary-materials
Abstract: Figure S1. Bio-ID screening reveals PI3Kβ, but not PI3Kα, as a selective interactor of EPHA2 in PTEN-null cancer cells. Figure S2. PTEN acts as a protein tyrosine phosphatase regulating PI3Kβ- EPHA2 interaction through dephosphorylation of tyrosine-962 (Y962) on PI3Kβ and impact tumorigenesis. Figure S3. Generation of a new antibody to detect phospho-PI3KβY962 levels. Figure S4. PI3Kβ and EPHA2 upregulate pERK/c-MYC and pAKT signaling in PTEN null cancer. Figure S5. Compound library screening identifies dasatinib as an inhibitor of PI3KβY962 phosphorylation that effectively inhibits PTEN-null tumor growth. Figure S6. Phosphorylation of PI3Kβ is a druggable target to treat PTEN-null tumors in vivo.
Authors: Shuang Tang, Qian Zhou, Johann S. Bergholz, Tao Jiang, Weihua Wang, Renlei Ji, Wendi Huang, Jiachen Wu, Yutong Li, Xiaochun Wan, Xiadi He, Qianchen Jing, Menghong Sun, Jared L. Johnson, Tomer M. Yaron-Barir, Da-Qiang Li, Bo Dai, Zefeng Wang, Xiaoling Li, Lewis C. Cantley, Thomas M. Roberts, Jean J. Zhao
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
OpenAlex ID: W7133222801