| First Author | Smrcka AV | Year | 1991 |
| Journal | Science | Volume | 251 |
| Issue | 4995 | Pages | 804-7 |
| PubMed ID | 1846707 | Mgi Jnum | J:30917 |
| Mgi Id | MGI:78201 | Doi | 10.1126/science.1846707 |
| Citation | Smrcka AV, et al. (1991) Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq. Science 251(4995):804-7 |
| abstractText | The hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C yields the second messengers inositol 1,4,5-trisphosphate (InsP3) and 1,2-diacylglycerol. This activity is regulated by a variety of hormones through G protein pathways. However, the specific G protein or proteins involved has not been identified. The alpha subunit of a newly discovered pertussis toxin-insensitive G protein (Gq) has recently been isolated and is now shown to stimulate the activity of polyphosphoinositide-specific phospholipase C (PI-PLC) from bovine brain. Both the maximal activity and the affinity of PI-PLC for calcium ion were affected. These results identify Gq as a G protein that regulates PI-PLC. |
