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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel.

Drosophila 14-3-3zeta (D14-3-3zeta) modulates the activity of the Slowpoke calcium-dependent potassium channel (dSlo) by interacting with the dSlo binding protein, Slob. We show here that D14-3-3zeta forms dimers in vitro. Site-directed mutations in its putative dimerization interface result in a dimerization-deficient form of D14-3-3zeta. Both the wild-type and dimerization-deficient forms of D14-3-3zeta bind to Slob with similar affinity and form complexes with dSlo. When dSlo and Slob are expressed in mammalian cells, the dSlo channel activity is similarly modulated by co-expression of either the wild-type or the dimerization-deficient form of D14-3-3zeta. In addition, dSlo is still modulated by wild-type D14-3-3zeta in the presence of a 14-3-3 mutant, which does not itself bind to Slob but forms heterodimers with the wild-type 14-3-3. These data, taken together, suggest that monomeric D14-3-3zeta is capable of modulating dSlo channel activity in this regulatory complex.[1]

References

  1. Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel. Zhou, Y., Reddy, S., Murrey, H., Fei, H., Levitan, I.B. J. Biol. Chem. (2003) [Pubmed]
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