A Single Residue in a Novel ADP-ribosyl Cyclase Controls Production of the Calcium-mobilizing Messengers Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate

Overview

Journal J Biol Chem

Specialty Biochemistry

Date 2010 Apr 14

PMID 20385553

Citations 5

Authors

Latha Ramakrishnan

Helene Muller-Steffner

Christophe Bosc

Victor D Vacquier

Francis Schuber

Marie-Jo Moutin

Leslie Dale

Sandip Patel

Affiliations

Soon will be listed here.

Abstract

Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate are ubiquitous calcium-mobilizing messengers produced by the same family of multifunctional enzymes, the ADP-ribosyl cyclases. Not all ADP-ribosyl cyclases have been identified, and how production of different messengers is achieved is incompletely understood. Here, we report the cloning and characterization of a novel ADP-ribosyl cyclase (SpARC4) from the sea urchin, a key model organism for the study of calcium-signaling pathways. Like several other members of the ADP-ribosyl cyclase superfamily, SpARC4 is a glycoprotein targeted to the plasma membrane via a glycosylphosphatidylinositol anchor. However, unlike most other members, SpARC4 shows a remarkable preference for producing cyclic ADP-ribose over nicotinic acid adenine dinucleotide phosphate. Mutation of a single residue (tyrosine 142) within a noncanonical active site reversed this striking preference. Our data highlight further diversification of this unusual enzyme family, provide mechanistic insight into multifunctionality, and suggest that different ADP-ribosyl cyclases are fine-tuned to produce specific calcium-mobilizing messengers.

Citing Articles

Characterization of ADP-ribosyl cyclase 1-like (ARC1-like) activity and NAADP signaling during slow muscle cell development in zebrafish embryos.

Kelu J, Webb S, Galione A, Miller A Dev Biol. 2018; 445(2):211-225.

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ADP-ribosyl cyclases regulate early development of the sea urchin.

Ramakrishnan L, Uhlinger K, Dale L, Hamdoun A, Patel S Messenger (Los Angel). 2017; 5(1-2):100-106.

PMID: 28529830 PMC: 5435102. DOI: 10.1166/msr.2016.1052.

Two-pore channels function in calcium regulation in sea star oocytes and embryos.

Ramos I, Reich A, Wessel G Development. 2014; 141(23):4598-609.

PMID: 25377554 PMC: 4302940. DOI: 10.1242/dev.113563.

Calcium pathway machinery at fertilization in echinoderms.

Ramos I, Wessel G Cell Calcium. 2012; 53(1):16-23.

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The signaling protein CD38 is essential for early embryonic development.

Churamani D, Geach T, Ramakrishnan L, Prideaux N, Patel S, Dale L J Biol Chem. 2012; 287(10):6974-8.

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