Data supporting the role of the non-glycosylated isoform of MIC26 in determining cristae morphology

Sebastian Koob; Miguel Barrera; Ruchika Anand; Andreas S Reichert

doi:10.1016/j.dib.2015.04.014

Data supporting the role of the non-glycosylated isoform of MIC26 in determining cristae morphology

Data Brief. 2015 May 18:4:135-9. doi: 10.1016/j.dib.2015.04.014. eCollection 2015 Sep.

Authors

Sebastian Koob¹, Miguel Barrera¹, Ruchika Anand², Andreas S Reichert³

Affiliations

¹ Mitochondrial Biology, Buchmann Institute of Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany.
² Institute of Biochemistry and Molecular Biology I, Heinrich Heine University, Medical Faculty, Universitätsstr. 1, 40225 Düsseldorf, Germany.
³ Mitochondrial Biology, Buchmann Institute of Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany ; Institute of Biochemistry and Molecular Biology I, Heinrich Heine University, Medical Faculty, Universitätsstr. 1, 40225 Düsseldorf, Germany.

Abstract

Membrane architecture is crucially important for mitochondrial function and integrity. The MICOS complex is located at crista junctions and determines cristae membrane morphology and the formation of crista junctions. Here we provide data of the bona fide MICOS subunit MIC26 for determining cristae morphology. MiRNA-mediated downregulation of MIC26 results in higher protein levels of MIC27 and in lower levels of Mic10. Using a miRNA-resistant form to MIC26 we show that this effect is specific to MIC26. Our data further demonstrate that depletion of MIC26 primarily affects the level of the 22 kDa mitochondrial isoform of MIC26 but not the amount of the secreted 55 kDa isoform of MIC26. Depletion of MIC27, however, increases secretion of the latter isoform. Overexpression of a myc-tagged version of MIC26 resulted in altered cristae morphology with swollen and partly vesicular cristae-structures.