Inhibition of Clathrin Assembly by High Affinity Binding of Specific Inositol Polyphosphates to the Synapse-specific Clathrin Assembly Protein AP-3
作者： Weilan Ye , Nawab Ali , Michael E. Bembenek , Stephen B. Shears , Eileen M. Lafer
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摘要: Bacterially expressed synapse-specific clathrin assembly protein, AP-3 (F1-20/AP180/NP185/pp155), bound with high affinity both inositol hexakisphosphate (InsP6) (Kd = 239 nM) and diphosphoinositol pentakisphosphate (PP-InsP5) 22 nM). The specificity of this ligand binding was demonstrated by competitive displacement [3H]InsP6. IC50 values were as follows: PP-InsP5 50 nM, InsP6 240 inositol-1,2,4,5,6-pentakisphosphate (Ins(1,2,4,5,6)P5) 2.2 μM, inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) 5 inositol-1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) > 10 inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) μM. Moreover, μM hexasulfate (InsS6) displaced only 15% physiological significance is the ligand-specific inhibition (PP-InsP5 Ins(1,2,4,5,6)P5); Ins(1,3,4,5,6)P5 InsS6 did not inhibit assembly. We also observed to purified bovine brain AP-3. separately 33-kDa amino terminus 58-kDa carboxyl terminus, it former that contained polyphosphate site. These studies suggest specific polyphosphates may play a role in regulation synaptic function interacting protein
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