We have previously demonstrated that relative levels of mito

We have previously demonstrated that relative levels of mitochondrial MIC26 and levels of secreted MIC26 can vary depending on the cell line investigated [1]. Here we show data deciphering whether depletion of MIC26 or MIC27 induces alterations in secreted levels of MIC26. Fig. 1B shows MIC26 depletion in 143B luliconazole with little influence on protein levels of secreted MIC26; here, depletion of MIC26 predominatly decreases the levels of its mitochondrial isoform (Fig. 1B). In contrast, protein levels of secreted MIC26 were markedly increased in 143B cells depleted for MIC27. Based on these findings we suggest that MIC27 is part of a regulatory pathway determining the amount of MIC26 within mitochondria and the amount of MIC255kDa being secreted. Fig. 2 shows that overexpression of myc-MIC26 leads to swollen or vesicle-like cristae in numerous mitochondrial sections. In control cells conventional cristae morphology with nicely tubular and ordered membranes were observed.
Specifications table
Value of the data
Experimental design – materials and methods
Specifications Table
Data, experimental design, materials and methods
Acknowledgements We would like to thank Rui Cheng for her precious technical assistance and Julie Klein for her help in the preparation of this manuscript. Support for this work was provided by Grants from the Belgian Program on Interuniversity Poles of Attraction initiated by the Belgian State (Prime Minister׳s Office, Science Policy Programming), the Fonds National de la Recherche Scientifique (F.R.S.-FNRS, Belgium, Télévie Grant number 7454313F; F.R.S.M. Grant number T.0022.14), the Fondation contre le Cancer (nonprofit organization, Belgium), the Fonds J. Maisin (Belgium), the Fondation Salus Sanguinis (Belgium), the Ludwig Institute for Cancer Research and WELBIO.
Specifications Table Value of the data Data The proteomes of Cyanothece sp. CCY 0110 grown in medium or medium supplemented with Cu2+ or Cd2+ were compared using two independent 8-plex iTRAQ studies (Fig. 1). For the chronic exposure, sub-lethal concentrations of 0.1mg/l of Cu2+ or 5mg/l of Cd2+ were used for 10 and 20 days, while in the acute experiment the cells were exposed to 10× these concentrations for 24h. In total, 202 (98 with two or more peptides) and 268 (130 with two or more peptides) proteins were identified and quantified for iTRAQ study 1 – Cu2+ and iTRAQ study 2 – Cd2+, respectively. The complete lists of peptides and proteins identified in iTRAQ studies 1 and 2 are provided in Supplementary Tables 1 and 2 respectively, and protein quantifications are provided in Supplementary Table 3. To identify groups of proteins (clusters) with similar variation patterns, hierarchical cluster analyses were performed. The strength of the analyses was improved by taking into account the ratios obtained for metal-exposed conditions compared to control, as well as those resulting from the comparison of different metal-exposed conditions (Fig. 1). This approach minimises the effects of over- or underestimated ratios and increases confidence. For each iTRAQ study, six statistically supported protein clusters (A–F) were formed (Figs. 2 and 3). Regarding study 1, 80% of proteins was included in cluster A1 (no significant change in any of the conditions tested), cluster B1 (no significant change in 10 and 20 days chronic exposure, and higher abundance in acute exposure) and cluster C1 (no significant change in 10 and 20 days chronic exposure, and lower abundance in acute exposure) (Fig. 2). Overall, the acute exposure of Cu2+ was the condition that promoted more quantitative proteome changes – 19%. Concerning study 2, 87% of the proteins were found in cluster A2 (no change in any of the conditions) and cluster B2 (lower abundance in 10 and 20 days chronic exposure) (Fig. 3). In contrast with what was observed for Cu2+, in study 2 the 10 and 20 days chronic exposure were the conditions that caused more differential protein expression, 12% and 13% respectively.