Dataset of integrin-linked kinase protein: Protein interactions in cardiomyocytes identified by mass spectrometry

Alexandra Traister; Mingliang Lu; John G Coles; Jason T Maynes

doi:10.1016/j.dib.2016.03.056

Dataset of integrin-linked kinase protein: Protein interactions in cardiomyocytes identified by mass spectrometry

Data Brief. 2016 Mar 19:7:1148-50. doi: 10.1016/j.dib.2016.03.056. eCollection 2016 Jun.

Authors

Alexandra Traister¹, Mingliang Lu¹, John G Coles¹, Jason T Maynes²

Affiliations

¹ Division of Cardiovascular Surgery, Hospital for Sick Children, Toronto, Ontario, Canada M5G 1X8.
² Department of Anesthesia and Pain Medicine, Hospital for Sick Children, Toronto, Ontario, Canada M5G 1X8; Departments of Anesthesia and Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 2J7.

Abstract

Using hearts from mice overexpressing integrin linked kinase (ILK) behind the cardiac specific promoter αMHC, we have performed immunoprecipitation and mass spectrometry to identify novel ILK protein:protein interactions that regulate cardiomyocyte activity and calcium flux. Integrin linked kinase complexes were captured from mouse heart lysates using a commercial antibody, with subsequent liquid chromatography tandem mass spectral analysis. Interacting partners were identified using the MASCOT server, and important interactions verified using reverse immunoprecipitation and mass spectrometry. All ILK interacting proteins were identified in a non-biased manner, and are stored in the ProteomeXchange Consortium via the PRIDE partner repository (reference ID PRIDE: PXD001053). The functional role of identified ILK interactions in cardiomyocyte function and arrhythmia were subsequently confirmed in human iPSC-cardiomyocytes.

Keywords: Calcium regulation; Cardiology; Mass spectrometry; Protein:protein interactions.