Interaction of oncoprotein transcription factor MYC with chromatin-associated protein host cell factor–1 controls expression of genes important for ribosome biogenesis and mitochondrial vigor, loss of which promotes tumor regression.

Differences in promoter affinity and MYC levels explain distinct expression profiles induced by physiological and oncogenic MYC.

We reveal TAPBPR is a peptide exchange catalyst which restricts the peptide repertoire presented by MHC I on cells, a finding which has important implications for all aspects of immune recognition.

Myc-dependent induction of amino acid transporter expression in response to T cell receptor activation is essential to enable T cell proteome remodelling upon immune activation.

The endoplasmic reticulum (ER) folding sensor UGGT1 essentially cooperates with the peptide editor TAPBPR to provide quality control of MHC I molecules in the antigen presentation pathway.

The number of different peptides presented by major histocompatibility complex class I molecules to the immune system's T lymphocytes is inversely correlated with cell surface expression and is strongly associated with the response to infectious disease.

A new potent and selective CDK9 inhibitor induces the expression of the proto-oncogene MYC via a mechanism that depends on the bromodomain protein BRD4.

The recently discovered peptide editor TAPBPR binds to UDP-glucose:glycoprotein glucosyltransferase 1 to provide quality control in the antigen presentation pathway by facilitating the reglucosylation of the glycan on MHC class I molecules.

MYC and Twist1 drive metastasis by a novel non-cell-autonomous transcriptional mechanism of eliciting a cytokinome that mediates the crosstalk between cancer cells and macrophages, and its therapeutic blockade inhibits metastasis.

Epstein-Barr virus controls B-cell growth and survival through large-scale reorganization of the enhancers of the MYC and BCL2L11 genes, and may promote MYC translocations as a result.