Oncogenesis: It's all about translation

sea-maid submitted, created time 4 weeks 1 day (www.nature.com)

The oncogene MYC regulates many cellular processes, making it difficult to pin down its precise function in driving tumor development. Maria Barna, David Ruggero and colleagues suggest that changes to cap-dependent and cap-independent translation during mitosis are pivotal.

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Specific tumor suppressor function for E2F2 in Myc-induced T cell lymphomagenesis

jimmy submitted, created time 1 year 3 months (www.pnas.org)

Deregulation of the Myc pathway and deregulation of the Rb pathway are two of the most common abnormalities in human malignancies. Recent in vitro experiments suggest a complex cross-regulatory relationship between Myc and Rb that is mediated through the control of E2F.

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Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells

Reviver submitted, created time 1 year 5 months (www.jcb.org)

"The idea that conversion of glucose to ATP is an attractive target for cancer therapy has been supported in part by the observation that glucose deprivation induces apoptosis in rodent cells transduced with the proto-oncogene MYC, but not in the parental line. Here, they found that depletion of glucose killed normal human cells irrespective of induced MYC activity and by a mechanism different from apoptosis. However, depletion of glutamine, another major nutrient consumed by cancer cells, induced apoptosis depending on MYC activity

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C-Terminal Modification Is Required for GABARAP-Mediated GABAA Receptor Trafficking

annatto submitted, created time 1 year 6 months (www.jneurosci.org)

"Western blotting with antibodies to v5 and myc revealed that the C terminus of GABARAP was cleaved off. Cleavage was blocked by mutating the C-terminal Gly116 to Ala, suggesting that G116 is required for the processing. Unlike ubiquitin, GABARAP was not incorporated covalently into higher-molecular-weight protein complexes. Nor was GABARAP degraded by ubiquitinylation through the proteasome, although GABARAP formed noncovalent dimers. Immunofluorescent confocal microscopy demonstrated that recombinantly expressed GABARAP was diffusely localized in PC12 cells

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