| First Author | von Weizsäcker E | Year | 1992 |
| Journal | Biochem Biophys Res Commun | Volume | 183 |
| Issue | 1 | Pages | 350-6 |
| PubMed ID | 1543505 | Mgi Jnum | J:21436 |
| Mgi Id | MGI:69413 | Doi | 10.1016/0006-291x(92)91650-f |
| Citation | von Weizsacker E, et al. (1992) Diversity among the beta subunits of heterotrimeric GTP-binding proteins: characterization of a novel beta-subunit cDNA. Biochem Biophys Res Commun 183(1):350-6 |
| abstractText | Heterotrimeric guanine nucleotide binding proteins transduce signals from cell surface receptors to intracellular effectors. The alpha subunit is believed to confer receptor and effector specificity on the G protein. This role is reflected in the diversity of genes that encode these subunits. The beta and gamma subunits are thought to have a more passive role in G protein function; biochemical data suggests that beta-gamma dimers are shared among the alpha subunits. However, there is growing evidence for active participation of beta-gamma dimers in some G protein mediated signaling systems. To further investigate this role, we examined the diversity of the beta subunit family in mouse. Using the polymerase chain reaction, we uncovered a new member of this family, G beta 4, which is expressed at widely varying levels in a variety of tissues. The predicted amino acid sequence of G beta 4 is 79% to 89% identical to the three previously known beta subunits. The diversity of beta gene products may be an important corollary to the functional diversity of G proteins. |
