The GSPT2 Knockout Jurkat Polyclonal Cells are a CRISPR/Cas9-edited population derived from Jurkat T lymphocytes, featuring targeted disruption of the GSPT2 gene. This polyclonal knockout composition captures a heterogeneous pool of gene-edited cells, providing a robust loss-of-function model suitable for translation termination studies. The polyclonal format offers experimental versatility without the need for clonal isolation, making it ideal for population-based assays and functional genomics screens.
Jurkat cells, originally isolated from a patient with acute lymphoblastic leukemia, represent an immortalized human T lymphocyte line extensively used in T cell signaling and leukemia research. They exhibit characteristic T cell activation pathways, including TCR-mediated signal transduction, and are a well-established model for investigating apoptosis, proliferation, and oncogenic transformation. Their leukemic origin renders them particularly relevant for mechanistic studies of T cell malignancies and for preclinical drug testing.
GSPT2 encodes the eukaryotic release factor 3 (eRF3a), a GTPase that collaborates with ETF1 (eRF1) to mediate translation termination at stop codons. Upon stop codon recognition, the eRF3a-eRF1-GTP complex promotes peptidyl-tRNA hydrolysis, releasing the nascent polypeptide. eRF3a activity is regulated by GTP binding and upstream signals including the mTOR pathway, while downstream it facilitates ribosome recycling by cooperating with ABCE1. Additionally, GSPT2 interfaces with the nonsense-mediated mRNA decay (NMD) machinery through interactions with UPF1 and PABPC1, linking translation termination to mRNA surveillance. Thus, GSPT2 disruption can lead to stop codon readthrough, perturbed protein synthesis, and activation of quality control pathways.
In Jurkat T cells, loss of GSPT2 function enables detailed interrogation of defective translation termination in a leukemic background. Impaired eRF3a activity can provoke ribosomal readthrough and accumulation of abnormal proteins, potentially altering cellular stress responses, apoptotic thresholds, and proliferation dynamics. As T cell leukemias may display translational dysregulation, this model provides a valuable platform to explore how termination fidelity influences leukemia pathogenesis. Moreover, the involvement of GSPT2 in ribosome recycling and NMD highlights its relevance to studies of translational quality control in cancer.
These cells support diverse experimental approaches, including dual-luciferase stop codon readthrough assays, puromycin incorporation measurements, and ribosome profiling to analyze translation. Co-immunoprecipitation can examine GSPT2 protein interactions, while flow cytometry and proliferation assays assess functional consequences. The polyclonal population is also well-suited for small-molecule screening targeting translational control or NMD. For further inquiries, contact Ascent Research.
