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The Journal of Neuroscience, May 1, 2002, 22(9):3342-3351

Regulation of Exocytosis through Ca²⁺/ATP-Dependent Binding of Autophosphorylated Ca²⁺/Calmodulin-Activated Protein Kinase II to Syntaxin 1A

Akihiro Ohyama^{1, 2}, Kohei Hosaka³, Yoshiaki Komiya¹, Kimio Akagawa⁴, Emiko Yamauchi^{5, 6}, Hisaaki Taniguchi^{5, 6}, Nobuyuki Sasagawa⁷, Konosuke Kumakura⁷, Sumiko Mochida⁸, Takashi Yamauchi⁹, and Michihiro Igarashi¹⁰

Departments of ¹ Molecular and Cellular Neurobiology and ² Anesthesiology and Reanimatology, Gunma University School of Medicine, and ³ Department of Basic Allied Medicine, Gunma University School of Health Sciences, Maebashi, Gunma 371-8511, Japan, ⁴ Department of Physiology, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan, ⁵ Division of Biomedical Polymer Sciences, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan, ⁶ Membrane Dynamics Project, Institute of Physical and Chemical Research (RIKEN) Harima Institute at Spring-8, Sayo, Hyogo 679-5148, Japan, ⁷ Life Science Institute, Sophia University, Chiyoda-ku, Tokyo 102-8554, Japan, ⁸ Department of Physiology, Tokyo Medical College, Shinjuku-ku, Tokyo 160-8402, Japan, ⁹ Department of Biochemistry, Faculty of Pharmaceutical Sciences, The University of Tokushima, Tokushima 770-8505, Japan, and ¹⁰ Division of Molecular and Cellular Biology, Department of Signal Transduction Research, Niigata University, Graduate School of Medical and Dental Sciences, Niigata, Niigata 951-8510, Japan

Syntaxin 1A/HPC-1 is a key component of the exocytotic molecular machinery, namely, the soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor mechanism. Although >10 syntaxin-binding proteins have been identified, they cannot completely explain the regulation of exocytosis. Thus, novel proteins may interact with syntaxin. Because exocytosis requires both Ca²⁺ and ATP, we searched for Ca²⁺/ATP-dependent syntaxin-binding proteins from the rat brain and discovered Ca²⁺/calmodulin-activated protein kinase II (CaMKII)-. At Ca²⁺ concentrations of >10⁶ M, only autophosphorylated CaMKII bound to syntaxin. Bound CaMKII was released from syntaxin by EGTA or by phosphatase, indicating that the binding is reversible. CaMKII bound to the linker domain of syntaxin, unlike any other known syntaxin-binding proteins. CaMKII-syntaxin complexes were also detected in synaptosomes by immunoprecipitation, and when reconstituted in vitro, they recruited larger amounts of synaptotagmin and SNAP-25 than syntaxin alone. The microinjected CaMKII-binding domain of syntaxin specifically affected exocytosis in chromaffin cells and in neurons. These results indicate that the Ca²⁺/ATP-dependent binding of CaMKII to syntaxin is an important process in the regulation of exocytosis.

Key words: syntaxin 1A/HPC-1; CaMKII; SNARE mechanism; exocytosis; linker domain; Munc-18

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Copyright © 2002 Society for Neuroscience  0270-6474/02/2293342-10$05.00/0

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