Proteins Cross-talking with Nox Complexes: The Social Life of Noxes

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2023
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SPRINGER INTERNATIONAL PUBLISHING
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de Bessa, T. C.; Laurindo, F. R. M.. Proteins Cross-talking with Nox Complexes: The Social Life of Noxes. In: . NADPH Oxidases Revisited: From Function to Structure: SPRINGER INTERNATIONAL PUBLISHING, 2023. p.379-396.
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Nox NADPH Oxidases exhibit a basic organization comprising a catalytic transmembrane subunit closely regulated by canonical regulatory subunits, discussed in other chapters of this book. However, many additional proteins regulate the expression, assembly, structure, activity and subcellular traffic of Nox subunits. As such, they gravitate around Nox complexes and physically associate with at least one among the regulatory or catalytic subunits. Given that such associated proteins, in turn, exert canonical effects distinct from Nox regulation, they connect Nox function to physiological cell programs, mediating cross-talk to and from Noxes. This chapter provides a systematic overview of proteins for which the physical interaction with Noxes has been validated by “wet-lab” experiments. Such proteins support both stimulatory or inhibitory effects towards several aspects of Nox regulation and can be roughly classified as: (a) kinase-related organizers; (b) general organizers; (c) chaperone-like organizers; (d) RhoGTPase and/or cytoskeleton-related organizers; (e) scaffold proteins. In addition, we provide an overview of the Nox interactome “in silico”, indicating that Noxes cross-talk with their environment preferentially via interactive protein hubs associated with their regulatory, rather than catalytic subunits. Characterizing the roles of Nox-associated proteins is essential to provide an integrative understanding of Noxes within multiple cellular physiological contexts. © The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Nature Switzerland AG 2023.
Palavras-chave
NADPH oxidase organizers, NADPH oxidases, Nox interactome, Nox-interacting proteins, P47phox, Poldip2, Protein-disulfide isomerase, Rac1, RhoGDI
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