| First Author | De Vries L | Year | 1999 |
| Journal | Trends Cell Biol | Volume | 9 |
| Issue | 4 | Pages | 138-44 |
| PubMed ID | 10203790 | Mgi Jnum | J:54103 |
| Mgi Id | MGI:1334101 | Doi | 10.1016/s0962-8924(99)01515-9 |
| Citation | De Vries L, et al. (1999) RGS proteins: more than just GAPs for heterotrimeric G proteins. Trends Cell Biol 9(4):138-44 |
| abstractText | Members of the newly described RGS family of proteins have a common RGS domain that contains GTPase-activating activity for many Galpha subunits of heterotrimeric G proteins. Their ability to dampen signalling via Galphai-, Galphaq- and Galpha12/13-coupled pathways makes them crucial players in mediating the multitude of cellular processes controlled by heterotrimeric G proteins. Some RGS proteins also contain additional motifs that link them to other signalling networks, where they constitute effector-type molecules. This review summarizes recent findings on RGS proteins, especially those that implicate RGS proteins in more than just enhancing the GTPase activity of their Galpha subunit targets. |
