ENAapplication/xmlftp://ftp.sra.ebi.ac.uk/vol1/fastq/SRR561/008/SRR5617738/SRR5617738.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/SRR561/007/SRR5617737/SRR5617737.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/SRR561/006/SRR5617736/SRR5617736.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/SRR561/005/SRR5617735/SRR5617735.fastq.gzprimaryOK200Genomicscity of hopehttps://www.ebi.ac.uk/ena/browser/view/PRJNA388202Mus musculusAlthough high c-Myc protein expression is observed alongside c-Myc gene amplification in some cancers, in most cases protein overexpression occurs while the amplified gene is largely absent, e.g. T-cell lymphoma (TCL). Here, Ca2+/calmodulin-dependent protein kinase II γ (CAMKIIγ) was shown to stabilize c-Myc protein by directly phosphorylating at serine 62 (S62), which represents a hitherto unknown mechanism of c-Myc protein overexpression. Further, CAMKIIγ was shown to be essential for tumor maintenance. Inhibiting CAMKIIγ with a potent CAMKIIγ-specific inhibitor destabilized c-Myc and reduced tumor burden dramatically. Importantly, high CAMKIIγ in clinical patient specimens positively correlated with increased c-Myc / pS62-c-Myc expression. Together, the CAMKIIγ:c-Myc axis critically influences the development and maintenance of TCL, and represent a novel therapeutic target for TCL. Overall design: We investigated how deleting CAMKIIγ suppressed the development of MNU-induced TCL in mice. Through RNA-sequencing, we analyzed the gene expression profiles of the thymuses of both wild-type and CAMKIIγ-/- mice, under either malignant (with MNU) or normal (without MNU) conditions.xref:PubMed:28697340ENAfalseMus musculusStabilization of c-Myc protein by CAMKIIγ promotes T-cell lymphoma2025-09-242017-05-31PRJNA388202GSE993641009028697340