The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Nox1-dependent Reactive Oxygen Generation Is Regulated by Rac1
Open accessAbstract
Rac1 has been implicated in the generation of reactive oxygen species (ROS) in several cell types, but the enzymatic origin of the ROS has not been proven. The present studies demonstrate that Nox1, a homolog of the phagocyte NADPH-oxidase component gp91(phox), is activated by Rac1. When Nox1 is co-expressed along with its regulatory subunits NOXO1 and NOXA1, significant ROS generation is seen. Herein, co-expression of constitutively active Rac1(G12V), but not wild-type Rac1, resulted in marked further stimulation of activity. Decreased Rac1 expression using small interfering RNA reduced Nox1-dependent ROS. CDC42(G12V) failed to increase activity, and small interfering RNA directed against CDC42 failed to decrease activity, pointing to specificity for Rac. TPR domain mutants of NOXA1 that interfere with Rac1 binding were ineffective in supporting Nox1-dependent ROS generation. Immunoprecipitation experiments demonstrated a complex containing Rac1(G12V), NOXO1, NOXA1, and Nox1. CDC42(G12V) could not substitute for Rac1(G12V) in such a complex. Nox1 formed a complex with Rac1(G12V) that was independent of NOXA1 and NOXO1, consistent with direct binding of Rac1(G12V) to Nox1. Rac1(G12V) interaction with NOXA1 was enhanced by Nox1 and NOXO1, suggesting cooperative binding. A model is presented comparing activation by regulatory subunits of Nox1 versus gp91(phox) (Nox2) in which Rac1 activation provides a major trigger that acutely activates Nox1-dependent ROS generation.
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Citations
Cites
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
Self-citationRHO GTPASES: Biochemistry and Biology
Jaffe, A. B., & Hall, A. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.020604.150721 · Cited by 3,009
Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.023 · Cited by 783
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
Rho family proteins and Ras transformation: the RHOad less traveled gets congested
Zohn, I. M., Campbell, S. L., Khosravi-Far, R., Rossman, K. L., & Der, C. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202181 · Cited by 352
Molecular basis for Rac2 regulation of phagocyte NADPH oxidase
Diebold, B. A., & Bokoch, G. M. (2001) · Nature Immunology · doi:10.1038/85259 · Cited by 318
Structure of the TPR Domain of p67phox in Complex with Rac·GTP
Lapouge, K., Smith, S. J. M., Walker, P. A., Gamblin, S. J., Smerdon, S. J., & Rittinger, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00091-2 · Cited by 311
Geiszt, M., Lekstrom, K., Witta, J., & Leto, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301289200 · Cited by 280
Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
ROS and the DNA damage response in cancer
Srinivas, U. S., Tan, B. W. Q., Vellayappan, B. A., & Jeyasekharan, A. D. (2019) · Redox Biology · doi:10.1016/j.redox.2018.101084 · Cited by 2,144
“γH2AX mediated activation of the Nox1-Rac1 complex [67,68] regulates ROS production [69].”
BackgroundThiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226
NADPH oxidase in brain injury and neurodegenerative disorders
Ma, M. W., Wang, J., Zhang, Q., Wang, R., Dhandapani, K. M., Vadlamudi, R. K., & Brann, D. W. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0150-7 · Cited by 432
Rac1 GTPase: A “Rac” of All Trades
Bosco, E. E., Mulloy, J. C., & Zheng, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8552-x · Cited by 350
DNA damage induces reactive oxygen species generation through the H2AX-Nox1/Rac1 pathway
Kang, M. A., So, E.-Y., Simons, A. L., Spitz, D. R., & Ouchi, T. (2012) · Cell Death & Disease · doi:10.1038/cddis.2011.134 · Cited by 311
“Flag-H2AX-overexpressing U2OS cells to inhibit the Rac1 GTPase, which is necessary for the activation of Nox1.(13)”
BackgroundInfluentialKim, K.-H., Chen, C.-C., Monzon, R. I., & Lau, L. F. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00049-13 · Cited by 261
Gianni, D., Taulet, N., Zhang, H., DerMardirossian, C., Kister, J., Martinez, L., Roush, W. R., Brown, S. J., Bokoch, G. M., & Rosen, H. (2010) · ACS Chemical Biology · doi:10.1021/cb100219n · Cited by 192
Lee, S. B., Bae, I. H., Bae, Y. S., & Um, H.-D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606702200 · Cited by 187
Receptor Activation of NADPH Oxidases
Petry, A., Weitnauer, M., & Görlach, A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.3026 · Cited by 162
Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain
Nisimoto, Y., Jackson, H. M., Ogawa, H., Kawahara, T., & Lambeth, J. D. (2010) · Biochemistry · doi:10.1021/bi9022285 · Cited by 161
Self-citationMalec, V., Gottschald, O. R., Li, S., Rose, F., Seeger, W., & Hänze, J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.008 · Cited by 149
SERRANDER, L., JAQUET, V, BEDARD, K., PLASTRE, O., HARTLEY, O., ARNAUDEAU, S., DEMAUREX, N., SCHLEGEL, W., & KRAUSE, K. (2007) · Biochimie · doi:10.1016/j.biochi.2007.05.004 · Cited by 146
Redox modifier genes in amyotrophic lateral sclerosis in mice
Marden, J. J., Harraz, M. M., Williams, A. J., Nelson, K., Luo, M., Paulson, H., & Engelhardt, J. F. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31265 · Cited by 145
Oxidative stress and antioxidants in the pathophysiology of malignant melanoma
Obrador, E., Liu-Smith, F., Dellinger, R. W., Salvador, R., Meyskens, F. L., & Estrela, J. M. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0327 · Cited by 119
Metadata
- Authors
- Cheng, G., Diebold, B. A., Hughes, Y., & Lambeth, J. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 281
- Issue
- 26
- Pages
- 17718-17726
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1985033865
- Cited by
- 277
- References
- 8
- FWCI
- 10.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
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