Sabina Visconti

TL;DR: The extreme end of AHA2 contains an unusual high-affinity binding site for 14-3-3 protein, which is in practice irreversible in the presence of fusicoccin.

TL;DR: Advances provided provide a framework of the understanding of plant hormone action, suggesting that 14-3-3 proteins act as hubs of a cellular web encompassing different signaling pathways, transducing and integrating diverse hormone signals in the regulation of physiological processes.

TL;DR: Control trypsin digestion of H+-ATPase abolished the association with GF14-6, a finding that was suggestive of an interaction with the C terminus of the enzyme.

TL;DR: In vivo experiments demonstrate that, among the different polyamines, spermine brings about 2-fold stimulation of the H(+)-ATPase activity and this effect is due to an increase in 14-3-3 levels associated with the enzyme.

TL;DR: Because the maximal conductance of KAT1 was unaffected by 14-3-3, it can exclude that these proteins act by increasing the number of channels, thus ruling out any effect of these proteins on channel trafficking and/or insertion into the oocyte membrane.