Sanford-Burnham Medical Research Institute, La Jolla, California 92037.
Sanford-Burnham Medical Research Institute, La Jolla, California 92037; Department of Pathology, University of California, San Diego California 92093.
J Biol Chem. 2014 Apr 11;289(15):10431-10444. doi: 10.1074/jbc.M113.541839. Epub 2014 Feb 28.
Most breast cancers are estrogen receptor-positive and treated with antiestrogens, but aberrant signaling networks can induce drug resistance. One of these networks involves the scaffolding protein BCAR1/p130CAS, which regulates cell growth and migration/invasion. A less investigated scaffolding protein that also confers antiestrogen resistance is the SH2 domain-containing protein BCAR3. BCAR1 and BCAR3 bind tightly to each other through their C-terminal domains, thus potentially connecting their associated signaling networks. However, recent studies using BCAR1 and BCAR3 interaction mutants concluded that association between the two proteins is not critical for many of their interrelated activities regulating breast cancer malignancy. We report that these previously used BCAR mutations fail to cause adequate loss-of-function of the complex. By using structure-based BCAR1 and BCAR3 mutants that lack the ability to interact, we show that BCAR3-induced antiestrogen resistance in MCF7 breast cancer cells critically depends on its ability to bind BCAR1. Interaction with BCAR3 increases the levels of phosphorylated BCAR1, ultimately potentiating BCAR1-dependent antiestrogen resistance. Furthermore, antiestrogen resistance in cells overexpressing BCAR1/BCAR3 correlates with increased ERK1/2 activity. Inhibiting ERK1/2 through overexpression of the regulatory protein PEA15 negates the resistance, revealing a key role for ERK1/2 in BCAR1/BCAR3-induced antiestrogen resistance. Reverse-phase protein array data show that PEA15 levels in invasive breast cancers correlate with patient survival, suggesting that PEA15 can override ERK1/2 activation by BCAR1/BCAR3 and other upstream regulators. We further uncovered that the BCAR3-related NSP3 can also promote antiestrogen resistance. Thus, strategies to disrupt BCAR1-BCAR3/NSP3 complexes and associated signaling networks could ultimately lead to new breast cancer therapies.
大多数乳腺癌是雌激素受体阳性的,并使用抗雌激素治疗,但异常信号网络会诱导耐药性。其中一个网络涉及支架蛋白 BCAR1/p130CAS,它调节细胞生长和迁移/侵袭。另一种较少研究的支架蛋白 BCAR3 也赋予抗雌激素耐药性。BCAR1 和 BCAR3 通过它们的 C 末端结构域紧密结合在一起,从而可能连接它们相关的信号网络。然而,最近使用 BCAR1 和 BCAR3 相互作用突变体的研究得出结论,两种蛋白质之间的关联对于它们许多相互关联的调节乳腺癌恶性活动不是关键的。我们报告说,这些先前使用的 BCAR 突变未能导致该复合物的充分功能丧失。通过使用缺乏相互作用能力的基于结构的 BCAR1 和 BCAR3 突变体,我们表明 BCAR3 在 MCF7 乳腺癌细胞中诱导的抗雌激素耐药性严重依赖于其与 BCAR1 结合的能力。与 BCAR3 的相互作用增加了磷酸化 BCAR1 的水平,最终增强了 BCAR1 依赖性抗雌激素耐药性。此外,过表达 BCAR1/BCAR3 的细胞中的抗雌激素耐药性与 ERK1/2 活性的增加相关。通过表达调节蛋白 PEA15 抑制 ERK1/2 可消除耐药性,揭示了 ERK1/2 在 BCAR1/BCAR3 诱导的抗雌激素耐药性中的关键作用。反相蛋白质阵列数据显示,侵袭性乳腺癌中的 PEA15 水平与患者的存活率相关,这表明 PEA15 可以通过 BCAR1/BCAR3 和其他上游调节剂来克服 ERK1/2 的激活。我们进一步发现,与 BCAR3 相关的 NSP3 也可以促进抗雌激素耐药性。因此,破坏 BCAR1-BCAR3/NSP3 复合物和相关信号网络的策略最终可能导致新的乳腺癌治疗方法。