Regulation of AP-2-synaptotagmin interaction by inositol high polyphosphates

Akihiro Mizutani, Mitsunori Fukuda, Michio Niinobe, Katsuhiko Mikoshiba

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


The inositol high-polyphosphate series (IHPS) inhibits neurotransmission through binding to the second C2 domain of synaptotagmins I and II(Syt), synaptic vesicle membrane proteins. We have revealed that several proteins, including α adaptins which are specific subunits of clathrin assembly protein, AP2, were eluted from mouse brain by affinity elution chromatography from the C2 domains of Syt II-immobilized Sepharose using 50 μM of InsP6. The interaction between Syt II and AP2 was more markedly inhibited by IHPS than by the same concentration of InsP3. Limited digestion of mouse crude synaptosomal fractions with trypsin revealed different cleavage patterns in the presence and absence of 50 μM InsP6. These results suggest that IHPS-binding to the C2B domain of synaptotagmin alters the state of protein-protein interaction including the synaptotagmin-AP2 interaction, possibly resulting in the inhibition of events involved in the synaptic vesicle trafficking.

Original languageEnglish
Pages (from-to)128-131
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 1997 Nov 7


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