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Originally published In Press as doi:10.1074/jbc.M008603200 on September 26, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40082-40087, December 22, 2000
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Neuronal Ca2+ Sensor-1/Frequenin Functions in an Autocrine Pathway Regulating Ca2+ Channels in Bovine Adrenal Chromaffin Cells*

Jamie L. Weiss, Deborah A. ArcherDagger , and Robert D. Burgoyne§

From The Physiological Laboratory, University of Liverpool, Crown Street, Liverpool, L69 3BX United Kingdom

NCS-1/frequenin belongs to a family of EF-hand-containing Ca2+ sensors expressed mainly in neurons. Overexpression of NCS-1/frequenin has been shown to stimulate neurotransmitter release but little else is known of its cellular roles. We have constructed an EF-hand mutant, NCS-1(E120Q), as a likely dominant inhibitor of cellular NCS-1 function. Recombinant NCS-1(E120Q) showed an impaired Ca2+-dependent conformational change but could still bind to cellular proteins. Transient expression of this mutant, but not NCS-1, in bovine adrenal chromaffin cells increased non-L-type Ca2+ channel currents. Cells expressing NCS-1(E120Q) no longer responded effectively to the removal of autocrine purinergic/opioid inhibition of Ca2+ currents but still showed voltage-dependent facilitation. These data are consistent with the existence of both voltage-dependent and voltage-independent pathways for Ca2+ channel inhibition in chromaffin cells. Our results suggest a novel function for NCS-1 specific for the voltage-independent autocrine pathway that negatively regulates non-L-type Ca2+ channels in chromaffin cells.

* This work was supported in part by a Wellcome Trust grant (to R. D. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a Wellcome Trust Prize Studentship.

§ To whom all correspondence should be addressed. Tel.: 44-151-794-5305; Fax: 44-151-794-5337; E-mail: burgoyne@liverpool.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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