ArticleThe Journal of biological chemistry2011
Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Type III CD38 is present in the membrane of neurosecretory vesicles and has a cytosol-facing catalytic domain in primate oxytocin neurons.Journal of neuroendocrinology · 2026Article
- cADPR is a gene dosage-sensitive biomarker of SARM1 activity in healthy, compromised, and degenerating axons.Experimental neurology · 2020Article
- CD38: An Immunomodulatory Molecule in Inflammation and Autoimmunity.Frontiers in immunology · 2020Review
- Resolving the topological enigma in CaThe Journal of biological chemistry · 2019Review
- The transferrin receptor CD71 regulates type II CD38, revealing tight topological compartmentalization of intracellular cyclic ADP-ribose production.The Journal of biological chemistry · 2019Article
- Authors' Reply: Pyridine nucleotide regulation of hepatic endoplasmic reticulum calcium uptake.Physiological reports · 2019Article
- A Cell-Permeant Mimetic of NMN Activates SARM1 to Produce Cyclic ADP-Ribose and Induce Non-apoptotic Cell Death.iScience · 2019Article
- A cytosolic chaperone complex controls folding and degradation of type III CD38.The Journal of biological chemistry · 2019Article
- CD38 produces nicotinic acid adenosine dinucleotide phosphate in the lysosome.The Journal of biological chemistry · 2018Article
- Characterization of CD38 in the major cell types of the heart: endothelial cells highly express CD38 with activation by hypoxia-reoxygenation triggering NAD(P)H depletion.American journal of physiology. Cell physiology · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Synthesis of the CaThe Journal of biological chemistry · 2017Article
- Cytosolic interaction of type III human CD38 with CIB1 modulates cellular cyclic ADP-ribose levels.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Immuno-targeting the multifunctional CD38 using nanobody.Scientific reports · 2016Article
- Depletion of NADP(H) due to CD38 activation triggers endothelial dysfunction in the postischemic heart.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Roles and mechanisms of the CD38/cyclic adenosine diphosphate ribose/Ca(2+) signaling pathway.World journal of biological chemistry · 2014Review
- Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization.The Journal of biological chemistry · 2012Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CD38 catalyzes the synthesis of cyclic ADP-ribose (cADPR), a Ca(2+) messenger responsible for regulating a wide range of physiological functions. It is generally regarded as an ectoenzyme, but its intracellular localization has also been well documented. It is not known if internal CD38 is enzymatically active and contributes to the Ca(2+) signaling function. In this study, we engineered a novel soluble form of CD38 that can be efficiently expressed in the cytosol and use cytosolic NAD as a substrate to produce cADPR intracellularly. The activity of the engineered CD38 could be decreased by mutating the catalytic residue Glu-226 and increased by the double mutation E146A/T221F, which increased its cADPR synthesis activity by >11-fold. Remarkably, the engineered CD38 exhibited the ability to form the critical disulfide linkages required for its enzymatic activity. This was verified by using a monoclonal antibody generated against a critical disulfide, Cys-254-Cys-275. The specificity of the antibody was established by x-ray crystallography and site-directed mutagenesis. The engineered CD38 is thus a novel example challenging the general belief that cytosolic proteins do not possess disulfides. As a further refinement of this approach, the engineered CD38 was placed under the control of tetracycline using an autoregulated construct. This study has set the stage for in vivo manipulation of cADPR metabolism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.