Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 38, Pages 31633-31640Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R112.349464
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Funding
- Research Grants Council of Hong Kong [768408, 769309, 770610, 771011]
- Natural Science Foundation of China (NSFC)/Research Grants Council (RGC) of Hong Kong Grant [N_HKU 722/08]
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Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate were discovered >2 decades ago. That they are second messengers for mobilizing Ca2+ stores has since been firmly established. Separate stores and distinct Ca2+ channels are targeted, with cyclic ADP-ribose acting on the ryanodine receptors in the endoplasmic reticulum, whereas nicotinic acid adenine dinucleotide phosphate mobilizes the endolysosomes via the two-pore channels. Despite the structural and functional differences, both messengers are synthesized by a ubiquitous enzyme, CD38, whose crystal structure and catalytic mechanism have now been well elucidated. How this novel signaling enzyme is regulated remains largely unknown and is the focus of this minireview.
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