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PLoS One 2007 Aug 29;28:e797. doi: 10.1371/journal.pone.0000797.
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Molecular characterization of a novel intracellular ADP-ribosyl cyclase.

Churamani D , Boulware MJ , Geach TJ , Martin AC , Moy GW , Su YH , Vacquier VD , Marchant JS , Dale L , Patel S .

BACKGROUND: ADP-ribosyl cyclases are remarkable enzymes capable of catalyzing multiple reactions including the synthesis of the novel and potent intracellular calcium mobilizing messengers, cyclic ADP-ribose and NAADP. Not all ADP-ribosyl cyclases however have been characterized at the molecular level. Moreover, those that have are located predominately at the outer cell surface and thus away from their cytosolic substrates. METHODOLOGY/PRINCIPAL FINDINGS: Here we report the molecular cloning of a novel expanded family of ADP-ribosyl cyclases from the sea urchin, an extensively used model organism for the study of inositol trisphosphate-independent calcium mobilization. We provide evidence that one of the isoforms (SpARC1) is a soluble protein that is targeted exclusively to the endoplasmic reticulum lumen when heterologously expressed. Catalytic activity of the recombinant protein was readily demonstrable in crude cell homogenates, even under conditions where luminal continuity was maintained. CONCLUSIONS/SIGNIFICANCE: Our data reveal a new intracellular location for ADP-ribosyl cyclases and suggest that production of calcium mobilizing messengers may be compartmentalized.

PubMed ID: 17726527
PMC ID: PMC1949048
Article link: PLoS One
Grant support: [+]

Species referenced: Echinodermata
Genes referenced: irak1bp1 LOC100887844 LOC100893907 LOC115919910 LOC373385 LOC574780 LOC576539 LOC581395 LOC593358 ngly1

Article Images: [+] show captions
References [+] :
Aarhus, Activation and inactivation of Ca2+ release by NAADP+. 1996, Pubmed, Echinobase