Identification of Pin1-Binding Phosphorylated Proteins in the Mouse Brain

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  • TATARA Yota
    Laboratory of Enzymology, Graduate School of Agricultural Science, Tohoku University Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine
  • TERAKAWA Takahiro
    Laboratory of Enzymology, Graduate School of Agricultural Science, Tohoku University Effector Cell Institute, Inc.
  • UCHIDA Takafumi
    Laboratory of Enzymology, Graduate School of Agricultural Science, Tohoku University

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To determine the role of Pin1 in the neurotransmission pathway, Pin1-binding proteins in mouse brain extract were identified. The Pin1-binding proteins were extracted from mouse brain homogenate, and the trypsin-digested peptides were analyzed by nano-liquid chromatography tandem mass spectrometry (LC-MS/MS). Proteins that involve the neurotransmission pathway, such as synapsin I, synapsin II, and calcium/calmodulin-dependent protein kinase type II (CaMKII), were identified in a Mascot search. Pull-down and immunoprecipitation assay indicated that Pin1 binds CaMKII in a phosphorylation-specific manner. It was assumed that Pin1 participates in the neurotransmission pathway involving the phosphorylation signal by CaMKII.

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