Mr. and Mrs. Ko Chi Ming Centre for Parkinson's Disease Research, School of Chinese Medicine, Hong Kong Baptist University, Hong Kong SAR, China; School of Chinese Medicine, Hong Kong Baptist University, Hong Kong SAR, China; Institute for Research and Continuing Education, Hong Kong Baptist University, Shenzhen, China.
Mr. and Mrs. Ko Chi Ming Centre for Parkinson's Disease Research, School of Chinese Medicine, Hong Kong Baptist University, Hong Kong SAR, China; School of Chinese Medicine, Hong Kong Baptist University, Hong Kong SAR, China.
Redox Biol. 2020 May;32:101445. doi: 10.1016/j.redox.2020.101445. Epub 2020 Jan 28.
TFEB (transcription factor EB) and TFE3 (transcription factor E3) are "master regulators" of autophagy and lysosomal biogenesis. The stress response p38 mitogen-activated protein (MAP) kinases affect multiple intracellular responses including inflammation, cell growth, differentiation, cell death, senescence, tumorigenesis, and autophagy. Small molecule p38 MAP kinase inhibitors such as SB202190 are widely used in dissection of related signal transduction mechanisms including redox biology and autophagy. Here, we initially aimed to investigate the links between p38 MAP kinase and TFEB/TFE3-mediated autophagy and lysosomal biogenesis. Unexpectedly, we found that only SB202190, rather than several other p38 inhibitors, promotes TFEB and TFE3 to translocate from the cytosol into the nucleus and subsequently enhances autophagy and lysosomal biogenesis. In addition, siRNA-mediated Tfeb and Tfe3 knockdown effectively attenuated SB202190-induced gene expression and lysosomal biogenesis. Mechanistical studies showed that TFEB and TFE3 activation in response to SB202190 is dependent on PPP3/calcineurin rather than on the inhibition of p38 or MTOR signaling, the main pathway for regulating TFEB and TFE3 activation. Importantly, SB202190 increased intracellular calcium levels, and calcium chelator BAPTAP-AM blocked SB202190-induced TFEB and TFE3 activation as well as autophagy and lysosomal biogenesis. Moreover, endoplasmic reticulum (ER) calcium is required for TFEB and TFE3 activation in response to SB202190. In summary, we identified a previously uncharacterized role of SB202190 in activating TFEB- and TFE3-dependent autophagy and lysosomal biogenesis via ER calcium release and subsequent calcium-dependent PPP3/calcineurin activation, leading to dephosphorylation of TFEB and TFE3. Given the importance of p38 MAP kinase invarious conditions including oxidative stress, the findings collectively indicate that SB202190 should not be used as a specific inhibitor for elucidating the p38 MAP kinase biological functions due to its potential effect on activating autophagy-lysosomal axis.
TFEB(转录因子 EB)和 TFE3(转录因子 E3)是自噬和溶酶体生物发生的“主调节因子”。应激反应 p38 丝裂原激活蛋白(MAP)激酶影响多种细胞内反应,包括炎症、细胞生长、分化、细胞死亡、衰老、肿瘤发生和自噬。小分子 p38 MAP 激酶抑制剂,如 SB202190,广泛用于解析包括氧化还原生物学和自噬在内的相关信号转导机制。在这里,我们最初旨在研究 p38 MAP 激酶与 TFEB/TFE3 介导的自噬和溶酶体生物发生之间的联系。出乎意料的是,我们发现只有 SB202190,而不是其他几种 p38 抑制剂,能够促进 TFEB 和 TFE3 从细胞质易位到细胞核,并随后增强自噬和溶酶体生物发生。此外,siRNA 介导的 Tfeb 和 Tfe3 敲低有效地减弱了 SB202190 诱导的基因表达和溶酶体生物发生。机制研究表明,SB202190 对 TFEB 和 TFE3 的激活依赖于 PPP3/钙调神经磷酸酶,而不是 p38 或 MTOR 信号通路,后者是调节 TFEB 和 TFE3 激活的主要途径。重要的是,SB202190 增加了细胞内钙水平,钙螯合剂 BAPTAP-AM 阻断了 SB202190 诱导的 TFEB 和 TFE3 激活以及自噬和溶酶体生物发生。此外,内质网(ER)钙是响应 SB202190 激活 TFEB 和 TFE3 所必需的。总之,我们确定了 SB202190 通过内质网钙释放和随后钙依赖性 PPP3/钙调神经磷酸酶激活来激活 TFEB 和 TFE3 依赖性自噬和溶酶体生物发生的以前未被描述的作用,导致 TFEB 和 TFE3 的去磷酸化。鉴于 p38 MAP 激酶在各种条件下的重要性,包括氧化应激,这些发现共同表明,由于其对激活自噬-溶酶体轴的潜在影响,SB202190 不应用作阐明 p38 MAP 激酶生物学功能的特异性抑制剂。