Philip Finly, Sahu Shriya, Caso Giuseppe, Scarlata Suzanne
Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Adv Biol Regul. 2013 Sep;53(3):319-30. doi: 10.1016/j.jbior.2013.07.002. Epub 2013 Jul 18.
Phospholipase C-β (PLCβ) enzymes are activated by G proteins in response to agents such as hormones and neurotransmitters, and have been implicated in leukemias and neurological disorders. PLCβ activity causes an increase in intracellular calcium which ultimately leads to profound changes in the cell. PLCβ localizes to three cellular compartments: the plasma membrane, the cytosol and the nucleus. Under most cell conditions, the majority of PLCβ localizes to the plasma membrane where it interacts with G proteins. In trying to determine the factors that localize PLCβ to the cytosol and nucleus, we have recently identified the binding partner, TRAX. TRAX is a nuclease and part of the machinery involved in RNA interference. This review discusses the interaction between PLCβ and TRAX, and its repercussions in G protein signaling and RNA silencing.
磷脂酶C-β(PLCβ)酶在诸如激素和神经递质等因子的作用下被G蛋白激活,并且与白血病和神经疾病有关。PLCβ的活性会导致细胞内钙含量增加,最终引起细胞发生深刻变化。PLCβ定位于三个细胞区室:质膜、胞质溶胶和细胞核。在大多数细胞条件下,大部分PLCβ定位于质膜,在那里它与G蛋白相互作用。在试图确定将PLCβ定位于胞质溶胶和细胞核的因素时,我们最近鉴定出了其结合伴侣TRAX。TRAX是一种核酸酶,是参与RNA干扰机制的一部分。本综述讨论了PLCβ与TRAX之间的相互作用及其在G蛋白信号传导和RNA沉默中的影响。