Roy Ananda L
Department of Pathology, Programs in Genetics and Immunology, Tufts University School of Medicine, 150 Harrison Avenue, Boston, Massachusetts 02111, USA.
ACS Chem Biol. 2006 Nov 21;1(10):619-22. doi: 10.1021/cb6004323.
In response to extracellular ligands, surface receptor tyrosine kinases and G-protein-coupled receptors activate isoforms of phospholipase C (PLC) and initiate calcium signaling. PLC can activate expression of surface transient receptor potential channels (TRPC) such as TRPC3, which modulate calcium entry through the plasma membrane. A recent paper shows that competitive binding of cytoplasmic TFII-I, a transcription factor, to PLC-gamma results in inhibition of TRPC3-mediated agonist-induced Ca(2+) entry. These results establish a novel cytoplasmic function for TFII-I.
作为对细胞外配体的响应,表面受体酪氨酸激酶和G蛋白偶联受体激活磷脂酶C(PLC)的同工型并启动钙信号传导。PLC可激活表面瞬时受体电位通道(TRPC)如TRPC3的表达,TRPC3可调节通过质膜的钙内流。最近一篇论文表明,细胞质转录因子TFII-I与PLC-γ的竞争性结合会抑制TRPC3介导的激动剂诱导的Ca(2+)内流。这些结果确立了TFII-I一种新的细胞质功能。