Proteomics

Dataset Information

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Complexome profiling of membrane fraction from Nox4 overexpressing HEK293 cells


ABSTRACT: Within the family of NADPH oxidases, Nox4 is unique as it is predominantly localized in the endoplasmic reticulum, has constitutive activity and generates H2O2. We hypothesize that these features are consequences of a so far unidentified Nox4-interacting protein. Blue native gel electrophoresis of solubilized membranes from HEK293 cells (overexpressing Nox4) separated macromolecular complexes containing Nox4. The combination of native gel electrophoresis and quantitative mass spectrometry was applied to identify proteins that co-migrate with Nox4. In addition, the data set contains information about macromolecular protein complexes in human cellular membranes that are stable to the solubilization with digitonin.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Ilka Wittig  

LAB HEAD: Ralf Brandes

PROVIDER: PXD003509 | Pride | 2017-04-07

REPOSITORIES: Pride

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Publications

The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein.

Prior Kim-Kristin KK   Wittig Ilka I   Leisegang Matthias S MS   Groenendyk Jody J   Weissmann Norbert N   Michalak Marek M   Jansen-Dürr Pidder P   Shah Ajay M AM   Brandes Ralf P RP  

The Journal of biological chemistry 20160209 13


Within the family of NADPH oxidases, NOX4 is unique as it is predominantly localized in the endoplasmic reticulum, has constitutive activity, and generates hydrogen peroxide (H2O2). We hypothesize that these features are consequences of a so far unidentified NOX4-interacting protein. Two-dimensional blue native (BN) electrophorese combined with SDS-PAGE yielded NOX4 to reside in macromolecular complexes. Interacting proteins were screened by quantitative SILAC (stable isotope labeling of amino a  ...[more]

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