A Kinase Divided.

Cancer Cell

Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address:

Published: August 2015

AI Article Synopsis

  • - Researchers, led by Herrero, discovered a small molecule that prevents the dimerization of ERK, which is important for cancer growth, without affecting its activity or MEK-induced phosphorylation.
  • - The study suggests that focusing on blocking protein dimerization is a promising new strategy for developing cancer treatments.
  • - This approach could help reduce drug resistance in kinases that are commonly involved in tumor signaling pathways.

Article Abstract

In this issue of Cancer Cell, Herrero and colleagues identify an anti-tumorigenic small molecule that blocks ERK dimerization, but neither its catalytic activity nor its phosphorylation by MEK. These findings demonstrate that targeting protein dimerization could be a therapeutic avenue for inhibiting kinase signaling pathways associated with lower drug resistance.

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Source
http://dx.doi.org/10.1016/j.ccell.2015.07.008DOI Listing

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