PMID: 9173888Apr 1, 1997Paper

N-terminal binding domain of Galpha subunits: involvement of amino acids 11-14 of Galphao in membrane attachment

The Biochemical Journal
L BusconiB M Denker

Abstract

Heterotrimeric guanine nucleotide binding proteins (G-proteins) transmit signals from membrane receptors to a variety of intracellular effectors. G-proteins reversibly associate with components of the signal transduction system, yet remain membrane attached throughout the cycle of activation. The Galpha subunits remain attached to the plasma membrane through a combination of factors that are only partially defined. We now demonstrate that amino acids within the N-terminal domain of Galpha subunits are involved in membrane binding. We used in vitro translation, a technique widely utilized to characterize functional aspects of G-proteins, and interactions with donor-acceptor membranes to demonstrate that amino acids 11-14 of Galphao contribute to membrane binding. The membrane binding of Galphao lacking amino acids 11-14 (D[11-14]) was significantly reduced at all membrane concentrations in comparison with wild-type Galphao. Several other N-terminal mutants of Galphao were characterized as controls, and these results indicate that differences in myristoylation, palmitoylation and betagamma interactions do not account for the reduced membrane binding of D[11-14]. Furthermore, when membrane attachment of Galphao and mutants was cha...Continue Reading

Citations

Jun 3, 2004·The Journal of Biological Chemistry·Zhixian ZhangTheodore G Wensel
Jul 2, 2003·Biochemistry·Hongzheng MaStephen G Graber

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