Mechanism of Ca2+ Activation of the NADPH Oxidase 5 (NOX5)
Open accessAbstract
NADPH oxidase 5 (NOX5) is a homologue of the gp91(phox) subunit of the phagocyte NADPH oxidase. NOX5 is expressed in lymphoid organs and testis and distinguished from the other NADPH oxidases by its unique N terminus, which contains three canonical EF-hands, Ca(2+)-binding domains. Upon heterologous expression, NOX5 was shown to generate superoxide in response to intracellular Ca(2+) elevations. In this study, we have analyzed the mechanism of Ca(2+) activation of NOX5. In a cell-free system, Ca(2+) elevations triggered superoxide production by NOX5 (K(m) = 1.06 microm) in an NADPH- and FAD-dependent but cytosol-independent manner. That result indicated a role for the N-terminal EF-hands in NOX5 activation. Therefore, we generated recombinant proteins of NOX5 N terminus and investigated their interactions with Ca(2+). Flow dialysis experiments showed that NOX5 N terminus contained four Ca(2+)-binding sites and allowed us to define the hitherto unidentified fourth, non-canonical EF-hand. The EF-hands of NOX5 formed two pairs: the very N-terminal pair had relatively low affinity for Ca(2+), whereas the more C-terminal pair bound Ca(2+) with high affinity. Ca(2+) binding caused a marked conformation change in the N terminus, which exposed its hydrophobic core, and became able to bind melittin, a model peptide for calmodulin targets. Using a pull-down assay, we demonstrate that the regulatory N terminus and the catalytic C terminus of NOX5 interact in a Ca(2+)-dependent way. Our results indicate that the Ca(2+)-induced conformation change of NOX5 N terminus led to enzyme activation through an intra-molecular interaction. That represents a novel mechanism of activation among NAD(P)H oxidases and Ca(2+)-activated enzymes.
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When Ca2+ is bound, the EF hands fold over the reductase CaM element to relieve autoinhibition.
“When Ca2+ is bound, the EF hands fold over the reductase CaM element to relieve autoinhibition (63, 944).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [63]
NADPH is the preferred substrate for all NOX isoforms, with the NOX2 isoform being particularly NADPH specific.
“NADPH is the preferred substrate for all NOX isoforms, with the NOX2 isoform being particularly NADPH specific (48, 63, 177, 1047).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [63]
The reductase domain of NOX5 includes a CaM-binding motif not found in the NOX1-4 proteins.
“The reductase domain of NOX5 also includes a CaM-binding motif not found in the NOX1–4 proteins.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [63]
NOX5 has a similar architecture to NOX1-4 but has an additional N-terminal domain before the transmembrane domain with four EF hand motifs that are responsive to Ca2+.
“NOX5 has a similar architecture but has an additional N-terminal domain before the transmembrane domain with four EF hand motifs that are responsive to Ca2+.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [63]
Cites
How to measure and predict the molar absorption coefficient of a protein
Pace, C., Vajdos, F., Fee, L. R., Grimsley, G., & Gray, T. (1995) · Protein Science · doi:10.1002/pro.5560041120 · Cited by 3,924 · see citing works
Calmodulin: a prototypical calcium sensor
Chin, D., & Means, A. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01800-6 · Cited by 1,531 · see citing works
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480 · see citing works
Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,166 · see citing works
[8] Reassessment of Ellman's reagent
Riddles, P. W., Blakeley, R. L., & Zerner, B. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(83)91010-8 · Cited by 1,099 · see citing works
Structure, function, and control of phosphoinositide-specific phospholipase C.
Rebecchi, M., & Pentyala, S. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1291 · Cited by 978 · see citing works
BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911 · see citing works
Gopalakrishna, R., & Anderson, W. B. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)90712-4 · Cited by 881 · see citing works
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840 · see citing works
Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820 · see citing works
Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
Zhang, M., Tanaka, T., & Ikura, M. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0995-758 · Cited by 696 · see citing works
A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622 · see citing works
Self-citationEF-hand calcium-binding proteins
Lewit‐Bentley, A., & Réty, S. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00142-1 · Cited by 568 · see citing works
Binding of Diffusible Molecules by Macromolecules: Rapid Measurement by Rate of Dialysis
Colowick, S. P., & Womack, F. C. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94419-4 · Cited by 517 · see citing works
A Novel Superoxide-producing NAD(P)H Oxidase in Kidney
Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y., & Sumimoto, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007597200 · Cited by 517 · see citing works
Two Novel Proteins Activate Superoxide Generation by the NADPH Oxidase NOX1
Bánfi, B., Clark, R. A., Steger, K., & Krause, K.-H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200613200 · Cited by 491 · see citing works
Self-citationSix Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)
Torres, M. Á. M., Onouchi, H., Hamada, S., Machida, C., Hammond-Kosack, K. E., & Jones, J. D. G. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00136.x · Cited by 424 · see citing works
Takeya, R., Ueno, N., Kami, K., Taura, M., Kohjima, M., Izaki, T., Nunoi, H., & Sumimoto, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212856200 · Cited by 380 · see citing works
Hosfield, C. M., Elce, J. S., Davies, P. L., & Jia, Z. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.6880 · Cited by 355 · see citing works
Ischemic stroke injury is reduced in mice lacking a functional NADPH oxidase
Walder, C. E., Green, S. P., Darbonne, W. C., Mathias, J., Rae, J., Dinauer, M. C., Curnutte, J. T., & Thomas, G. R. (1997) · Stroke · doi:10.1161/01.str.28.11.2252 · Cited by 349 · see citing works
Regulation of the Erythropoietin Gene
Ebert, B. L., & Bunn, H. F. (1999) · Blood · doi:10.1182/blood.v94.6.1864 · Cited by 335 · see citing works
A Mammalian H + Channel Generated Through Alternative Splicing of the NADPH Oxidase Homolog NOH-1
Bánfi, B., Maturana, A. D., Jaconi, S., Arnaudeau, S., Laforge, T., Sinha, B. N. M., Ligeti, E., Demaurex, N., & Krause, K. (2000) · Science · doi:10.1126/science.287.5450.138 · Cited by 309 · see citing works
Self-citationRegulation of the Erythropoietin Gene
Imagawa, S., Goldberg, M. A., & Bunn, H. F. (1989) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0623-8_9 · Cited by 298 · see citing works
Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
Lambeth, J. D. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00003 · Cited by 282 · see citing works
Geiszt, M., Lekstrom, K., Witta, J., & Leto, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301289200 · Cited by 280 · see citing works
NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells
Brar, S. S., Corbin, Z. A., Kennedy, T. P., Hemendinger, R. A., Thornton, L., Bommarius, B., Arnold, R. S., Whorton, A. R., Sturrock, A., Huecksteadt, T. P., et al. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00525.2002 · Cited by 259 · see citing works
Structures of the troponin C regulatory domains in the apo and calcium-saturated states
Gagné, S. M., Tsuda, S., Li, M. X., et al. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0995-784 · Cited by 220 · see citing works
Blanchard, H., Grochulski, P., Li, Y., et al. (1997) · Nature Structural Biology · doi:10.1038/nsb0797-532 · Cited by 208 · see citing works
NAD(P)H Oxidase-Derived Reactive Oxygen Species as Mediators of Angiotensin II Signaling
Hanna, I. R., Taniyama, Y., Szöcs, K., Ročić, P., & Griendling, K. K. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602762197443 · Cited by 194 · see citing works
Ca2+-dependent high-affinity complex formation between calmodulin and melittin
Comte, M., Maulet, Y., & Cox, J. A. (1983) · Biochemical Journal · doi:10.1042/bj2090269 · Cited by 191 · see citing works
Self-citationGuidebook to the Calcium-binding Proteins
Celio, M. R. (1996) · doi:10.1093/oso/9780198599517.001.0001 · Cited by 182 · see citing works
NADPH oxidase subunit, gp91phox homologue, preferentially expressed in human colon epithelial cells
Kikuchi, H., Hikage, M., Miyashita, H., & Fukumoto, M. (2000) · Gene · doi:10.1016/s0378-1119(00)00258-4 · Cited by 161 · see citing works
Guidebook to the calcium binding proteins
(1998) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(98)90012-x · Cited by 137 · see citing works
Palicz, A., Foubert, T. R., Jesaitis, A. J., Maródi, L., & McPhail, L. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007759200 · Cited by 116 · see citing works
Dang, P. M., Cross, A. R., & BABIOR, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061029698 · Cited by 109 · see citing works
Qualliotine‐Mann, D., Agwu, D. E., Ellenburg, M. D., McCall, C. E., & McPhail, L. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80462-1 · Cited by 97 · see citing works
Role for NADPH/NADH Oxidase in the Modulation of Vascular Tonea
Münzel, T. F., Hink, U., Heitzer, T. A., & Meinertz, T. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb09253.x · Cited by 96 · see citing works
Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex.
Atkinson, R. A., Joseph, C., Kelly, G. P., Muskett, F. W., Frenkiel, T. A., Nietlispach, D., & Pastore, A. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-853 · Cited by 91 · see citing works
Changing the Conformation State of Cytochrome b 558 Initiates NADPH Oxidase Activation
Berthier, S., Paclet, M., Lerouge, S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209755200 · Cited by 91 · see citing works
Dinauer, M. C., & Orkin, S. H. (1992) · Annual Review of Medicine · doi:10.1146/annurev.me.43.020192.001001 · Cited by 89 · see citing works
Ca2+ Signaling Modulates Cytolytic T Lymphocyte Effector Functions
Esser, M. T., Haverstick, D. M., Fuller, C. L., Gullo, C. A., & Braciale, V. L. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.7.1057 · Cited by 85 · see citing works
Miloš, M., Schaer, J., Comte, M., et al. (1986) · Biochemistry · doi:10.1021/bi00368a067 · Cited by 81 · see citing works
Structure of Apoptosis-Linked Protein ALG-2
Jia, J., Tarabykina, S., Hansen, C., Berchtold, M. W., & Cygler, M. (2001) · Structure · doi:10.1016/s0969-2126(01)00585-8 · Cited by 79 · see citing works
Cation‐ and peptide‐binding properties of human centrin 2
Durussel, I., Blouquit, Y., Middendorp, S., et al. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01452-6 · Cited by 77 · see citing works
Self-citationRole of Prenylation in the Interaction of Rho-Family Small GTPases with GTPase Activating Proteins
Molnár, G., Dagher, M., Geiszt, M., et al. (2001) · Biochemistry · doi:10.1021/bi011158e · Cited by 72 · see citing works
Self-citationIlari, A., Johnson, K. A., Nastopoulos, V., et al. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2002.5417 · Cited by 68 · see citing works
Sarcoplasmic calcium-binding protein
Hermann, A., & Cox, J. A. (1995) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(94)00218-j · Cited by 65 · see citing works
Self-citationBrändle, D., Bilsborough, J., Rülicke, T., Uyttenhove, C., Boon, T., & den Eynde, B. J. V. (1998) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199812)28:12 · Cited by 62 · see citing works
Shatwell, K. P., & Segal, A. W. (1996) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(96)00084-2 · Cited by 59 · see citing works
Jia, J., Han, Q., Borregaard, N., Lollike, K., & Cygler, M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3925 · Cited by 49 · see citing works
Durussel, I., Luan-Rilliet, Y., Petrova, T. V., et al. (1993) · Biochemistry · doi:10.1021/bi00060a034 · Cited by 33 · see citing works
Self-citationSperm binding to the human zona pellucida and calcium influx in response to GnRH and progesterone
Morales, P. J., Pizarro, E., Kong, M., et al. (2002) · Andrologia · doi:10.1046/j.1439-0272.2002.00510.x · Cited by 14 · see citing works
Cation- and Peptide-Binding Properties of Human Calmodulin-like Skin Protein
Durussel, I., Méhul, B., Bernard, D., et al. (2002) · Biochemistry · doi:10.1021/bi016062z · Cited by 13 · see citing works
Self-citationSperm binding to the human zona pellucida and calcium influx in response to GnRH and progesterone
Morales, P. J., Pizarro, E., Kong, M., et al. (2002) · Andrologia · doi:10.1111/j.1439-0272.2002.tb02945.x · Cited by 8 · see citing works
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Self-citationThe NOX toolbox: validating the role of NADPH oxidases in physiology and disease
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Singh, D. K., Kumar, D., Siddiqui, Z., Basu, S. K., Kumar, V., & Rao, K. V. S. (2005) · Cell · doi:10.1016/j.cell.2005.02.036 · Cited by 206 · see citing works
Montezano, A. C., Burger, D., Paravicini, T. M., Chignalia, A. Z., Yusuf, H., Almasri, M., He, Y., Callera, G. E., He, G., Krause, K.-H., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.216036 · Cited by 188 · see citing works
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- Authors
- Bánfi, B., Tirone, F., Durussel, I., Knisz, J., Moskwa, P., Molnár, G. Z., Krause, K.-H., & Cox, J. A.
- Affiliations
- University of Geneva (CH)
- University Hospital of Geneva (CH)
- Semmelweis University (HU)
- Corresponding author
- Cox, Jos A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-04
- Volume
- 279
- Issue
- 18
- Pages
- 18583-18591
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2105940831
- Cited by
- 389
- References
- 54
- Citations by year
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- FWCI
- 7.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion)
- Funders
- National Institute on Aging (R01AG019519, AG19519)
- National Institute of Allergy and Infectious Diseases (AI 20866, R01AI020866)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase 5, calcium activation, EF-hand, superoxide production, calcium binding sites, conformational change, intramolecular interactions
- MeSH terms
- NADPH Oxidase 5, Amino Acid Sequence, Binding Sites, Calcium, Cell Line, Cell-Free System, Enzyme Activation, Humans, Kinetics, Melitten, Membrane Proteins, Peptide Fragments, Protein Conformation, Superoxides, NADPH Oxidases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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