Year: 2007
Type: article
Abstract: 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.
Source: PLoS ONE
Language: English
Subfield: Physiology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,382
Awards: BIOCHEMISTRY OF SPERM-EGG INTERACTION AND FERTILIZATION, G2010519799, Functional architecture of IP3-evoked local Ca2+signals, G4608216649, Molecular and Functional Characterisation of Sea Urchin ADP-ribosyl Cyclases, CAREER: Application of Fluorescence-Based Tools in Research and Educational Domains - Illuminating Local Ca2+ Signals in Cells and DNA-Based Methods in Local Schools, G6983277863
OpenAlex ID: W2134524949