MassIVE MSV000094329

Complete Public PXD050667

Affinity Purification Mass Spectrometry of protein protein interactors with alternatively-spliced Uromodulin

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Description

We identified an alternatively spliced UMOD which is uniquely localized intracellularly. This intracellular isoform enhanced mitochondrial function. To understand its molecular mechanism, we performed affinity-purification coupled to mass spectrometry using MDCK cell lysate expressing UMOD variant. We prepared MDCK cells which express mock (negative control), wild-type human UMOD or alternatively spliced human UMOD. UMOD was isolated by Immunoprecipitation and interacting proteins were identified by mass spectrometry proteomics analysis. [doi:10.25345/C5WM14502] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: uromodulin ; MDCK ; protein protein interactions

Contact

Principal Investigators:
(in alphabetical order) 		Amber L. Mosley, Indiana University School of Medicine, USA
Tarek M. El-Achkar, Indiana University School of Medicine, USA
Submitting User: edoud

Publications

Nanamatsu A, Rhodes GJ, LaFavers KA, Micanovic R, Lazar V, Khan S, Barwinska D, Makino S, Zollman A, Cheng YH, Doud EH, Mosley AL, Repass MJ, Kamocka MM, Baride A, Phillips CL, Kelly KJ, Eadon MT, Himmelfarb J, Kretzler M, Bacallao RL, Dagher PC, Hato T, El-Achkar TM.
Alternative splicing of uromodulin enhances mitochondrial metabolism for adaptation to stress in kidney epithelial cells.
J Clin Invest. Epub 2025 Apr 8.

ashkar.
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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