Kazlauskas Andrius
Schepens Eye Research Institute, Massachusetts Eye and Ear Infirmary, Harvard Medical School, Boston, Massachusetts, USA
Mol Cell Biol. 2014 Oct;34(20):3778-9. doi: 10.1128/MCB.00968-14. Epub 2014 Aug 11.
While growth factor-driven dimerization of receptor tyrosine kinases (RTKs) is a simple and intuitive mechanism of activating RTKs, K.-I. Arimoto et al. (Mol. Cell. Biol. 34:3843-3854, 2014, doi:10.1128/MCB.00758-14) describe a novel means of promoting the activity of RTKs. Namely, plakophilin-2 (PKP2) associates with the epidermal growth factor receptor (EGFR) and enhances its ligand-dependent and ligand-independent activity. This discovery suggests that antagonizing PKP2 may be a new therapeutic opportunity to combat tumors in which activation of EGFR contributes to pathogenesis.
虽然生长因子驱动的受体酪氨酸激酶(RTK)二聚化是激活RTK的一种简单直观的机制,但有本光一等人(《分子与细胞生物学》34:3843 - 3854,2014年,doi:10.1128/MCB.00758 - 14)描述了一种促进RTK活性的新方法。具体而言,桥粒芯蛋白2(PKP2)与表皮生长因子受体(EGFR)结合,并增强其依赖配体和不依赖配体的活性。这一发现表明,拮抗PKP2可能是对抗EGFR激活促成发病机制的肿瘤的一个新的治疗机会。