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Molecular characterization of a novel cell surface ADP-ribosyl cyclase from the sea urchin. Cell Signal 2008 Dec;20(12):2347-55



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Pubmed Central ID




Scopus ID

2-s2.0-55049128821   12 Citations


The sea urchin is an extensively used model system for the study of calcium signalling by the messenger molecules NAADP and cyclic ADP-ribose. Both are synthesized by ADP-ribosyl cyclases but our molecular understanding of these enzymes in the sea urchin is limited. We have recently reported the cloning of an extended family of sea urchin ADP-ribosyl cyclases and shown that one of these enzymes (SpARC1) is active within the endoplasmic reticulum lumen. These studies suggest that production of messengers is compartmentalized. Here we characterize the properties of SpARC2. SpARC2 catalyzed both NAADP and cyclic ADP-ribose production. Unusually, the NAD surrogate, NGD was a poor substrate. In contrast to SpARC1, heterologously expressed SpARC2 localized to the plasma membrane via a glycosylphosphatidylinositol (GPI)-anchor. Transcripts for SpARC2 were readily detectable in sea urchin eggs and a majority of the endogenous membrane bound activity was found to be GPI-anchored. Our data reveal striking differences in the properties of sea urchin ADP-ribosyl cyclases and provide further evidence that messenger production may occur outside of the cytosol.

Author List

Churamani D, Boulware MJ, Ramakrishnan L, Geach TJ, Martin AC, 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
Base Sequence
Cells, Cultured
Cyclic ADP-Ribose
Microscopy, Fluorescence
Sea Urchins
Type C Phospholipases
Xenopus laevis
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a