| First Author | Lyon AM | Year | 2011 |
| Journal | Nat Struct Mol Biol | Volume | 18 |
| Issue | 9 | Pages | 999-1005 |
| PubMed ID | 21822282 | Mgi Jnum | J:245254 |
| Mgi Id | MGI:5914607 | Doi | 10.1038/nsmb.2095 |
| Citation | Lyon AM, et al. (2011) An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galphaq activation. Nat Struct Mol Biol 18(9):999-1005 |
| abstractText | The enzyme phospholipase C-beta (PLCbeta) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the Gq family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCbeta (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCbeta3 considerably increase basal activity and diminish stimulation by Galphaq. Galphaq binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCbeta. |
