C-terminal tail of NADPH oxidase organizer 1 (Noxo1) mediates interaction with NADPH oxidase activator (Noxa1) in the NOX1 complex

Shrestha, Pravesh; Yun, Ji Hye; Ko, Yoon Joo; Kim, Myeongkyu; Lee, Weontae

doi:10.1016/j.bbrc.2017.06.083

Cited by 6 publications

(10 citation statements)

References 31 publications

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“…Other groups have characterized similar interactions with the SH3 domain and other proline-rich proteins and refer to this surface region as the specificity zone (24). We saw significant chemical shift perturbations of the residues in the ␤4 strand and the RT loop that are conserved across many SH3 domains (25), suggesting that these residues are important for SH3 function. Residues Asp-23 and Leu-24 in the RT loop of Fyn-SH3 showed large chemical shift perturbations in the presence of hnRNPA2 266 -341.…”

Section: Discussionmentioning

confidence: 65%

“…Residues Asp-23 and Leu-24 in the RT loop of Fyn-SH3 showed large chemical shift perturbations in the presence of hnRNPA2 266 -341. Chemical shift perturbations were observed in these same conserved residues of Noxa1-SH3 upon binding of Noxo1 proline-rich region (25). Another study claims that the binding of Fyn-SH3 to proline-rich proteins is mediated by weak interactions between the hydroxyl groups of the tyrosines in the n-Src loop region of SH3 and the backbone of the proline residues (26).…”

Section: Discussionmentioning

confidence: 92%

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The SH3 domain of Fyn kinase interacts with and induces liquid–liquid phase separation of the low-complexity domain of hnRNPA2

Amaya¹,

Ryan

Fawzi³

2018

Journal of Biological Chemistry

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Liquid-liquid phase separation of proteins and nucleic acids into membraneless organelles (MLOs) spatially organizes cellular components and reactions. The RNA-binding protein heterogeneous nuclear ribonucleoprotein A2 (hnRNPA2) carries mRNA targets in MLOs called transport granules in neurons and oligodendrocytes. At sites of local translation, hnRNPA2 is phosphorylated by the tyrosine protein kinase Fyn, releasing the mRNA for translation. Fyn recognizes targets through its SH3 domain (Fyn-SH3). However, hnRNPA2 lacks canonical SH3binding sequences, raising the question of how Fyn-SH3 binds hnRNPA2 in phase-separated transport granules. Here, we characterize the structural details of the interaction of the hnRNPA2 low-complexity domain (LC) with Fyn-SH3 and the effect of Fyn-SH3 on hnRNPA2 phase separation. We combined in vitro microscopy and solution NMR spectroscopy to evaluate assembly of hnRNPA2 and Fyn-SH3 into in vitro phase-separated granules and probe the structural details of their interaction. We observed that Fyn-SH3 induces hnRNPA2 LC phase separation and that Fyn-SH3 is incorporated into in vitro hnRNPA2 LC granules. Moreover, we identified hnRNPA2 LC interaction sites on the surface of Fyn-SH3. Our data offer a structural view of how hnRNPA2 LC may interact with Fyn. To our knowledge, our study provides the first example of a single globular domain inducing phase separation of a disordered MLO scaffold protein.

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Section: Discussionmentioning

confidence: 65%

Section: Discussionmentioning

confidence: 92%

The SH3 domain of Fyn kinase interacts with and induces liquid–liquid phase separation of the low-complexity domain of hnRNPA2

Amaya¹,

Ryan

Fawzi³

2018

Journal of Biological Chemistry

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“…Various members of the NOX family, namely NOX1-5, Duox1 and Duox2, are present in tissues [6][7][8]. The interaction between Nox organizer 1 (Noxo1) and Nox activator 1 (Noxa1 SH3) is required for O2 ⋅− formation by NOX1, as shown in Figure 1a [9]. Our group previously showed that the SH3 domain of Noxa1 SH3 interacts with the C-terminal region of Noxo1 in the NOX1 complex, see Figure 1b [9].…”

Section: Introductionmentioning

confidence: 90%

Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study

Attri

Park

Backer

et al. 2020

International Journal of Biological Macromolecules

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“…Nox1: This NADPH oxidase isoform was the first non-phagocytic isoform to be discovered displaying 58% amino acid sequence identity to the phagocyte enzyme [ 35 – 37 ]. Activity depends on p22 and on the p47 and p67 homologs, NOXO1 and NOXA1, respectively [ 38 , 39 ]. It is located on the X chromosome of the human and mouse genome [ 40 ] and is preferentially expressed in human colon epithelial cells [ 38 ].…”

Section: Introductionmentioning

confidence: 99%

“…Loss of Nox1 can cause inflammatory bowel disease [ 47 ], as can certain defects in Nox2 expression (discussed above). Regulatory subunits of Nox1 in colon cells (NOXO1, NOXA1) have been identified and are distinct from the regulatory subunits of Nox2 [ 39 ]. Through interaction with ADAM17, Nox1 is reponsible for the growth and metastasis of certain forms of colon cancer [ 48 ].…”

Section: Introductionmentioning

confidence: 99%

The defense and signaling role of NADPH oxidases in eukaryotic cells

Breitenbach

Rinnerthaler

Weber

et al. 2018

Wien Med Wochenschr

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SummaryThis short review article summarizes what is known clinically and biochemically about the seven human NADPH oxidases. Emphasis is put on the connection between mutations in the catalytic and regulatory subunits of Nox2, the phagocyte defense enzyme, with syndromes like chronic granulomatous disease, as well as a number of chronic inflammatory diseases. These arise paradoxically from a lack of reactive oxygen species production needed as second messengers for immune regulation. Both Nox2 and the six other human NADPH oxidases display signaling functions in addition to the functions of these enzymes in specialized biochemical reactions, for instance, synthesis of the hormone thyroxine. NADPH oxidases are also needed by Saccharomyces cerevisiae cells for the regulation of the actin cytoskeleton in times of stress or developmental changes, such as pseudohyphae formation. The article shows that in certain cancer cells Nox4 is also involved in the re-structuring of the actin cytoskeleton, which is required for cell mobility and therefore for metastasis.

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C-terminal tail of NADPH oxidase organizer 1 (Noxo1) mediates interaction with NADPH oxidase activator (Noxa1) in the NOX1 complex

Cited by 6 publications

References 31 publications

The SH3 domain of Fyn kinase interacts with and induces liquid–liquid phase separation of the low-complexity domain of hnRNPA2

The SH3 domain of Fyn kinase interacts with and induces liquid–liquid phase separation of the low-complexity domain of hnRNPA2

Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study

The defense and signaling role of NADPH oxidases in eukaryotic cells

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