High impact information on Slob

• The results provide evidence for a dSlo/Slob/14-3-3 regulatory protein complex [1].
• We have found that there are several Slob proteins, resulting from multiple translational start sites and alternative splicing, and have named them based on their molecular weights (in kD) [2].
• Mass spectrometric and mutational analysis demonstrates that the major site of phosphorylation by PKAc within Slob is serine 54 [3].
• The slowpoke channel binding protein Slob from Drosophila melanogaster exhibits regulatable protein kinase activity [3].
• The phosphorylation of histone is enhanced markedly when Slob is pretreated with the catalytic subunit of cyclic AMP-dependent protein kinase (PKAc) [3].

Biological context of Slob

• The amino terminus of Slob, Slowpoke channel binding protein, critically influences its modulation of the channel [2].
• The results are consistent with the hypothesis that Slob exhibits regulatable protein kinase activity, whose activity is enhanced by phosphorylation at serine 54 [3].
• The slowpoke channel binding protein Slob from Drosophila melanogaster contains a putative protein kinase domain within its amino acid sequence [3].

Associations of Slob with chemical compounds

• Mechanisms of Two Modulatory Actions of the Channel-binding Protein Slob on the Drosophila Slowpoke Calcium-dependent Potassium Channel [4].
• The enhancement of Slob kinase activity by PKAc pretreatment is eliminated when serine 54 in Slob is mutated to alanine (S54A) [3].

Physical interactions of Slob

• Both the wild-type and dimerization-deficient forms of D14-3-3zeta bind to Slob with similar affinity and form complexes with dSlo [5].

Other interactions of Slob

• Coimmunoprecipitation experiments from Drosophila heads and transfected cells confirm that 14-3-3 interacts with dSlo via Slob [1].
• A yeast two-hybrid screen with Slob as bait identifies the zeta isoform of 14-3-3 as a Slob-binding protein [1].

References