Proteomics

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NCLX proximity biotinylation screen


ABSTRACT: The mitochondrial sodium/calcium exchanger, NCLX, is critical to maintaining mitochondrial calcium homeostasis, yet little remains known about the mechanisms regulating its function. Here, we performed proximity biotinylation screening to identify the NCLX interactome and potential protein regulators of NCLX function by expressing a human NCLX-BioID2 fusion protein, or BioID2 alone, in AC16 cardiomyocytes and in HeLa cells. Biotinylated proteins were identified via affinity purification mass spectrometry.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: John Elrod  

PROVIDER: MSV000093004 | MassIVE |

SECONDARY ACCESSION(S): PXD045834

REPOSITORIES: MassIVE

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The balance between mitochondrial calcium (<sub>m</sub>Ca<sup>2+</sup>) uptake and efflux is essential for ATP production and cellular homeostasis. The mitochondrial sodium-calcium exchanger, NCLX, is a critical route of <sub>m</sub>Ca<sup>2+</sup> efflux in excitable tissues, such as the heart and brain, and animal models support NCLX as a promising therapeutic target to limit pathogenic <sub>m</sub>Ca<sup>2+</sup> overload. However, the mechanisms that regulate NCLX activity are largely unknow  ...[more]

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