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Molecular characterization of a novel intracellular ADP-ribosyl cyclase. PLoS One 2007 Aug 29;2(8):e797 PMID: 17726527 PMCID: PMC1949048


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.

Author List

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


Jonathan S. Marchant PhD Chair, Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

ADP-ribosyl Cyclase
Amino Acid Sequence
Calcium Signaling
Cloning, Molecular
Cyclic ADP-Ribose
Endoplasmic Reticulum
Molecular Sequence Data
Protein Isoforms
Sea Urchins
Sequence Alignment

View this publication's entry at the Pubmed website PMID: 17726527
jenkins-FCD Prod-130 96200611f8481f0aa4f84230b11dd74d063847a3