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M201132200v1
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Papers In Press, published online ahead of print May 28, 2002
J. Biol. Chem, 10.1074/jbc.M201132200
Submitted on February 4, 2002
Revised on April 23, 2002
Accepted on May 28, 2002

Mechanisms underlying the neuronal calcium sensor-1-evoked enhancement of exocytosis in PC12 cells

Schuichi Koizumi, Patrizia Rosa, Gary B. Willars, R.A. John Challiss, Elena Taverna, Maura Francolini, Martin D. Bootman, Peter Lipp, Kazuhide Inoue, John Roder, and Andreas Jeromin

Section of Neuropharmacology, Department of Pharmacology, National Institute of Health Sciences, Tokyo 158-8501

Corresponding Author: skoizumi{at}nihs.go.jp

Neuronal calcium sensor-1 (NCS-1), or originally identified homologue frequenin, belongs to a superfamily of EF-hand calcium binding proteins. Although NCS-1 is thought to enhance synaptic efficacy or exocytosis mainly by activating ion channel function, the detail molecular basis for the enhancement is still a matter of debate. Here, mechanisms underlying the NCS-1-evoked enhancement of exocytosis were investigated using PC12 cells overexpressing NCS-1. NCS-1 was found to have a broad distribution in the cells being partially distributed in the cytosol and associated to vesicles and tubular-like structures. Biochemical and immunohistochemical studies indicated that NCS-1 partially colocalized with the light synaptic-vesicle marker synaptophysin. When stimulated with uridine 5'-triphosphate (UTP) or bradykinin, agonists to phospholipase C (PLC)-linked receptors, NCS-1 enhanced the agonist-mediated elementary and global Ca2+ signaling and increased the levels of downstream signals of phosphatidylinositol 4-kinase (PtdIns4K). NCS-1 enhanced the UTP-evoked exocytosis but not the depolarization-evoked Ca2+ responses or exocytosis, suggesting that the enhancement by NCS-1 should involve PLC-linked receptor-mediated signals rather than the Ca2+ channels or exocytotic machinery per se. Taken together NCS-1 enhances phosphoinositide turnover, resulting in enhancement of Ca2+ signaling and exocytosis. This is a novel regulatory mechanism of exocytosis that might involve the activation of PtdInd4K.


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