Scarlata Suzanne
Department of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Rd., Worcester, MA, 01609, United States.
Adv Biol Regul. 2019 Aug;73:100636. doi: 10.1016/j.jbior.2019.100636. Epub 2019 Jul 29.
Phospholipase Cβ (PLCβ) is a signaling enzyme activated by G proteins to generate calcium signals. The catalytic core of PLCβ is surrounded by modular domains that mediate the interaction of the enzyme with known protein partners on the plasma membrane. The C-terminal region PLCβ contains a novel coiled-coil domain that is required for Gαq binding and activation. Recent work has shown that this domain also binds a number of cytosolic proteins that regulate protein translation, and that these proteins compete with Gαq for PLCβ binding. The ability of PLCβ to shuttle between the cytosol to impact protein translation and the plasma membrane to mediate calcium signals puts PLCβ in a central role in cell function.
磷脂酶Cβ（PLCβ）是一种由G蛋白激活以产生钙信号的信号酶。PLCβ的催化核心被模块化结构域包围，这些结构域介导该酶与质膜上已知蛋白质伴侣的相互作用。PLCβ的C末端区域包含一个新型卷曲螺旋结构域，这是Gαq结合和激活所必需的。最近的研究表明，该结构域还结合了许多调节蛋白质翻译的胞质蛋白，并且这些蛋白质与Gαq竞争PLCβ的结合。PLCβ在胞质溶胶之间穿梭以影响蛋白质翻译以及在质膜上介导钙信号的能力，使PLCβ在细胞功能中发挥核心作用。
