Transcription factor TFII-I conducts a cytoplasmic orchestra.
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.
Roy
Ananda L
AL
Department of Pathology, Programs in Genetics and Immunology, Tufts University School of Medicine, 150 Harrison Avenue, Boston, Massachusetts 02111, USA. ananda.roy@tufts.edu
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D035463:Pol1 Transcription Initiation Complex Proteins / Q000502:physiology*; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D019473:Transcription Factors, TFII / Q000502:physiology*; D014158:Transcription, Genetic; D010738:Type C Phospholipases / Q000378:metabolism*
D008024:Ligands; D035463:Pol1 Transcription Initiation Complex Proteins; D020033:Protein Isoforms; D019473:Transcription Factors, TFII; D010738:Type C Phospholipases; D002118:Calcium