TY  - JOUR
A1  - Koob, Sebastian
A1  - Barrera, Miguel
A1  - Anand, Ruchika
A1  - Reichert, Andreas
T1  - Data supporting the role of the non-glycosylated isoform of MIC26 in determining cristae morphology
T2  - Data in Brief
N2  - 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.
Y1  - 2015
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/53506
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-535064
SN  - 2352-3409
N1  - Copyright © 2015 The Authors. Under a Creative Commons license https://creativecommons.org/licenses/by/4.0/
VL  - 4
SP  - 135
EP  - 139
PB  - Elsevier
CY  - Amsterdam [u. a.]
ER  -