Replication Data for: Complex effects of PKM2 and of PKM2:IP3R disruption on intracellular Ca2+ handling and cellular functions

Datasets that support the figures published in Lemos et al., Cells (2023). The project aims to elucidate the role of the metabolic enzyme PKM2 in intracellular Ca2+ signaling. We demonstrated that PKM2 can differentially regulate cytosolic and mitochondrial Ca2+ handling. In the cytosol, PKM2 interacts with and inhibits IP3R activity, while in the mitochondria, PKM2 modulates the Ca2+ signal by influencing mitochondrial metabolism, structure, and dynamics. By using the TAT-D5SD peptide, corresponding to amino acids 2078-2098 of IP3R1, which disrupts the PKM2:IP3R complex, we observed that the effects of this peptide on Ca2+ handling and apoptosis depend on the IP3R but not on PKM2. Furthermore, the presence of PKM1 and the tyrosine kinase Lck is not required, suggesting the presence of one or more other proteins that can interact with the IP3R and form a complex at the same site as PKM2 on the IP3R.本数据集用于支撑Lemos等人2023年发表于《Cells》期刊的配图内容。本研究旨在阐明代谢酶丙酮酸激酶M2（PKM2）在细胞内钙信号传导中的作用。研究证实，PKM2可差异性调控胞质与线粒体的钙稳态调控过程。在胞质中，PKM2可与肌醇三磷酸受体（IP3R）结合并抑制其活性；而在线粒体中，PKM2通过影响线粒体代谢、结构与动力学过程来调控钙信号。本研究使用了对应于肌醇三磷酸受体1（IP3R1）2078-2098位氨基酸的TAT-D5SD肽，该肽可破坏PKM2与IP3R的复合物。实验观察到，该肽对钙稳态调控与细胞凋亡的影响依赖于IP3R，而非PKM2。此外，丙酮酸激酶M1（PKM1）与酪氨酸激酶Lck的存在并非必需，这提示存在一种或多种其他蛋白质，可与IP3R结合，并在IP3R上与PKM2相同的位点形成复合物。