Identification of MYC as an antinecroptotic protein that stifles RIPK1-RIPK3 complex formation

The underlying mechanism of necroptosis in relation to cancer is still unclear. Here, MYC, a potent oncogene, is an antinecroptotic factor that directly suppresses the formation of the RIPK1-RIPK3 complex. Gene set enrichment analyses reveal that the MYC pathway is the most prominently down-regulated signaling pathway during necroptosis. Depletion or deletion of MYC promotes the RIPK1-RIPK3 interaction, thereby stabilizing the RIPK1 and RIPK3 proteins and facilitating necroptosis. Interestingly, MYC binds to RIPK3 in the cytoplasm and inhibits the interaction between RIPK1 and RIPK3 in vitro. Furthermore, MYC-nick, a truncated form that is mainly localized in the cytoplasm, prevented TNF-induced necroptosis. Finally, down-regulation of MYC enhances necroptosis in leukemia cells and suppresses tumor growth in a xenograft model upon treatment with birinapant and emricasan. MYC-mediated suppression of necroptosis is a mechanism of necroptosis resistance in cancer, and approaches targeting MYC to induce necroptosis represent an attractive therapeutic strategy for cancer

Study of Refining Effect of Mixed Pulps Using Refiner Plates with Different Bar Patterns

A new lightweight vertical bar plate was developed by inserting individual bars into the plate base rather than the typical sand casting method. The lightweight vertical bar plate has a very sharp bar edge because vertical bars are inserted instead of trapezoidal bars. The refining effects of the mixed stock with softwood bleached kraft pulp (Sw-BKP) and hardwood bleached kraft pulp (Hw-BKP) were compared using two types of lightweight vertical bar plates with cutting edge lengths of 55 km/s (PA55) and 97 km/s (PB97). The fine bar plate (PB97) with large CEL (PB97) was very effective in reducing the refining energy required to reach the final freeness regardless of the mixing ratios of Sw-BKP and Hw-BKP compared to the plate with a small CEL (PA55). PB97 also consumed less refining energy than PA55 until proper sheet strength was achieved. In particular, irrespective of the mixing ratios of Sw-BKP and Hw-BKP, the tensile strength of sheets at the final freeness was greater in PB97 than in PA55. For stock throughput during refining, PA55 with the wide groove was almost similar to PB97 with the narrow groove

BWMK1, a Rice Mitogen-Activated Protein Kinase, Locates in the Nucleus and Mediates Pathogenesis-Related Gene Expression by Activation of a Transcription Factor

Mitogen-activated protein kinase (MAPK) cascades are known to transduce plant defense signals, but the downstream components of the MAPK have as yet not been elucidated. Here, we report an MAPK from rice (Oryza sativa), BWMK1, and a transcription factor, OsEREBP1, phosphorylated by the kinase. The MAPK carries a TDY phosphorylation motif instead of the more common TEY motif in its kinase domain and has an unusually extended C-terminal domain that is essential to its kinase activity and translocation to the nucleus. The MAPK phosphorylates OsEREBP1 that binds to the GCC box element (AGCCGCC) of the several basic pathogenesis-related gene promoters, which in turn enhances DNA-binding activity of the factor to the cis element in vitro. Transient co-expression of the BWMK1 and OsEREBP1 in Arabidopsis protoplasts elevates the expression of the β-glucuronidase reporter gene driven by the GCC box element. Furthermore, transgenic tobacco (Nicotiana tabacum) plants overexpressing BWMK1 expressed many pathogenesis-related genes at higher levels than wild-type plants with an enhanced resistance to pathogens. These findings suggest that MAPKs contribute to plant defense signal transduction by phosphorylating one or more transcription factors