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Qiang Xue, Haifeng Pei, Qinshe Liu, Mingjun Zhao, Jing Sun, Erhe Gao, Xinliang Ma, Ling Tao
Mitochondrial Ca(2+) overload is a main contributor to mitochondrial damage hence cardiomyocyte death in myocardial ischemia/reperfusion (MI/R) injury. MICU1 has been recently identified as an important regulator of mitochondrial Ca(2+) homeostasis. Here we try to identify the role of MICU1 in MI/R, and to investigate whether the mitochondrial importer receptor Tom70 possesses critical roles in the mitochondrial translocation of MICU1 and MI/R. Specific small interfering RNA (20 μg) against MICU1 and Tom70, and lentivirus vectors carrying the Tom70a sequences (3...
July 13, 2017: Cell Death & Disease
Juan Antonio Martos-Sitcha, Azucena Bermejo-Nogales, Josep Alvar Calduch-Giner, Jaume Pérez-Sánchez
BACKGROUND: Acclimation to abiotic challenges, including decreases in O2 availability, requires physiological and anatomical phenotyping to accommodate the organism to the environmental conditions. The retention of a nucleus and functional mitochondria in mature fish red blood cells makes blood a promising tissue to analyse the transcriptome and metabolic responses of hypoxia-challenged fish in an integrative and non-invasive manner. METHODS: Juvenile gilthead sea bream (Sparus aurata) were reared at 20-21 °C under normoxic conditions (> 85% O2 saturation) followed by exposure to a gradual decrease in water O2 concentration to 3...
2017: Frontiers in Zoology
Chen Kang, Jingping Qin, Wil Osei, Keli Hu
Protein kinase C (PKC) is an important mediator in the cardioprotection of ischemic preconditioning and has been shown to translocate to mitochondria upon activation. However, little is known about the cellular signaling underlying the translocation of PKC isoforms to mitochondria and its age-dependence. The present study aimed to explore whether adenosine-induced translocation of PKCε to mitochondria is mediated by caveolin-3 and/or adenosine A2B receptor/PI3 kinase mediated signaling, and whether the mitochondrial targeting of PKCε is age-related...
January 22, 2017: Biochemical and Biophysical Research Communications
Hai-Feng Pei, Juan-Ni Hou, Fei-Peng Wei, Qiang Xue, Fan Zhang, Cheng-Fei Peng, Yi Yang, Yue Tian, Juan Feng, Jin Du, Lei He, Xiu-Chuan Li, Er-He Gao, De Li, Yong-Jian Yang
Mitochondrial dysfunction leads to reactive oxygen species (ROS) overload, exacerbating injury in myocardial infarction (MI). As a receptor for translocases in the outer mitochondrial membrane (Tom) complex, Tom70 has an unknown function in MI, including melatonin-induced protection against MI injury. We delivered specific small interfering RNAs against Tom70 or lentivirus vectors carrying Tom70a sequences into the left ventricles of mice or to cultured neonatal murine ventricular myocytes (NMVMs). At 48 h post-transfection, the left anterior descending coronary arteries of mice were permanently ligated, while the NMVMs underwent continuous hypoxia...
January 2017: Journal of Pineal Research
Hoda Hoseini, Saroj Pandey, Tobias Jores, Anja Schmitt, Mirita Franz-Wachtel, Boris Macek, Johannes Buchner, Kai Stefan Dimmer, Doron Rapaport
Most mitochondrial proteins are synthesized in the cytosol prior to their import into the organelle. It is commonly accepted that cytosolic factors are required for delivering precursor proteins to the mitochondrial surface and for keeping newly synthesized proteins in an import-competent conformation. However, the identity of such factors and their defined contribution to the import process are mostly unknown. Using a presequence-containing model protein and a site-directed photo-crosslinking approach in yeast cells we identified the cytosolic chaperones Hsp70 (Ssa1) and Hsp90 (Hsp82) as well as their cochaperones, Sti1 and Ydj1, as putative cytosolic factors involved in mitochondrial protein import...
September 2016: FEBS Journal
Leticia M Zanphorlin, Tatiani B Lima, Michael J Wong, Tiago S Balbuena, Conceição A S A Minetti, David P Remeta, Jason C Young, Leandro R S Barbosa, Fabio C Gozzo, Carlos H I Ramos
To accomplish its crucial role, mitochondria require proteins that are produced in the cytosol, delivered by cytosolic Hsp90, and translocated to its interior by the translocase outer membrane (TOM) complex. Hsp90 is a dimeric molecular chaperone and its function is modulated by its interaction with a large variety of co-chaperones expressed within the cell. An important family of co-chaperones is characterized by the presence of one TPR (tetratricopeptide repeat) domain, which binds to the C-terminal MEEVD motif of Hsp90...
September 2, 2016: Journal of Biological Chemistry
Monika Sinzel, Tao Tan, Philipp Wendling, Hubert Kalbacher, Cagakan Özbalci, Xenia Chelius, Benedikt Westermann, Britta Brügger, Doron Rapaport, Kai Stefan Dimmer
Mitochondria are separated from the remainder of the eukaryotic cell by the mitochondrial outer membrane (MOM). The MOM plays an important role in different transport processes like lipid trafficking and protein import. In yeast, the ER-mitochondria encounter structure (ERMES) has a central, but poorly defined role in both activities. To understand the functions of the ERMES, we searched for suppressors of the deficiency of one of its components, Mdm10, and identified a novel mitochondrial protein that we named Mdm10 complementing protein 3 (Mcp3)...
July 2016: EMBO Reports
Adam L Hughes, Casey E Hughes, Kiersten A Henderson, Nina Yazvenko, Daniel E Gottschling
Mitochondrial dysfunction is a hallmark of aging, and underlies the development of many diseases. Cells maintain mitochondrial homeostasis through a number of pathways that remodel the mitochondrial proteome or alter mitochondrial content during times of stress or metabolic adaptation. Here, using yeast as a model system, we identify a new mitochondrial degradation system that remodels the mitochondrial proteome of aged cells. Unlike many common mitochondrial degradation pathways, this system selectively removes a subset of membrane proteins from the mitochondrial inner and outer membranes, while leaving the remainder of the organelle intact...
April 20, 2016: ELife
Julia Sauerwald, Tobias Jores, Michal Eisenberg-Bord, Silvia Gabriela Chuartzman, Maya Schuldiner, Doron Rapaport
A special group of mitochondrial outer membrane (MOM) proteins spans the membrane several times via multiple helical segments. Such multispan proteins are synthesized on cytosolic ribosomes before their targeting to mitochondria and insertion into the MOM. Previous work recognized the import receptor Tom70 and the mitochondrial import (MIM) complex, both residents of the MOM, as required for optimal biogenesis of these proteins. However, their involvement is not sufficient to explain either the entire import pathway or its regulation...
September 2015: Molecular and Cellular Biology
Pei-Hsuan Lin, Hsien-Yi Lin, Cheng-Chin Kuo, Liang-Tung Yang
BACKGROUND: The epidermis forms a critical barrier that is maintained by orchestrated programs of proliferation, differentiation, and cell death. Gene mutations that disturb this turnover process may cause skin diseases. Human GASDERMIN A (GSDMA) is frequently silenced in gastric cancer cell lines and its overexpression has been reported to induce apoptosis. GSDMA has also been linked with airway hyperresponsiveness in genetic association studies. The function of GSDMA in the skin was deduced by dominant mutations in mouse gasdermin A3 (Gsdma3), which caused skin inflammation and hair loss...
June 24, 2015: Journal of Biomedical Science
Małgorzata Wojtkowska, Dorota Buczek, Olgierd Stobienia, Andonis Karachitos, Monika Antoniewicz, Małgorzata Slocinska, Wojciech Makałowski, Hanna Kmita
Protein import into mitochondria requires a wide variety of proteins, forming complexes in both mitochondrial membranes. The TOM complex (translocase of the outer membrane) is responsible for decoding of targeting signals, translocation of imported proteins across or into the outer membrane, and their subsequent sorting. Thus the TOM complex is regarded as the main gate into mitochondria for imported proteins. Available data indicate that mitochondria of representative organisms from across the major phylogenetic lineages of eukaryotes differ in subunit organization of the TOM complex...
July 2015: Protist
Andrew Murley, Reta D Sarsam, Alexandre Toulmay, Justin Yamada, William A Prinz, Jodi Nunnari
Organelle contact sites perform fundamental functions in cells, including lipid and ion homeostasis, membrane dynamics, and signaling. Using a forward proteomics approach in yeast, we identified new ER-mitochondria and ER-vacuole contacts specified by an uncharacterized protein, Ylr072w. Ylr072w is a conserved protein with GRAM and VASt domains that selectively transports sterols and is thus termed Ltc1, for Lipid transfer at contact site 1. Ltc1 localized to ER-mitochondria and ER-vacuole contacts via the mitochondrial import receptors Tom70/71 and the vacuolar protein Vac8, respectively...
May 25, 2015: Journal of Cell Biology
Jonathan Melin, Markus Kilisch, Piotr Neumann, Oleksandr Lytovchenko, Ridhima Gomkale, Alexander Schendzielorz, Bernhard Schmidt, Thomas Liepold, Ralf Ficner, Olaf Jahn, Peter Rehling, Christian Schulz
The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove...
August 2015: Biochimica et Biophysica Acta
Daniel O Frank, Jörn Dengjel, Florian Wilfling, Vera Kozjak-Pavlovic, Georg Häcker, Arnim Weber
The pro-apoptotic Bcl-2-family protein Bim belongs to the BH3-only proteins known as initiators of apoptosis. Recent data show that Bim is constitutively inserted in the outer mitochondrial membrane via a C-terminal transmembrane anchor from where it can activate the effector of cytochrome c-release, Bax. To identify regulators of Bim-activity, we conducted a search for proteins interacting with Bim at mitochondria. We found an interaction of Bim with Tom70, Tom20 and more weakly with Tom40, all components of the Translocase of the Outer Membrane (TOM)...
2015: PloS One
Jan Mani, Silvia Desy, Moritz Niemann, Astrid Chanfon, Silke Oeljeklaus, Mascha Pusnik, Oliver Schmidt, Carolin Gerbeth, Chris Meisinger, Bettina Warscheid, André Schneider
Mitochondrial protein import is essential for all eukaryotes and mediated by hetero-oligomeric protein translocases thought to be conserved within all eukaryotes. We have identified and analysed the function and architecture of the non-conventional outer membrane (OM) protein translocase in the early diverging eukaryote Trypanosoma brucei. It consists of six subunits that show no obvious homology to translocase components of other species. Two subunits are import receptors that have a unique topology and unique protein domains and thus evolved independently of the prototype receptors Tom20 and Tom70...
2015: Nature Communications
Kyle Bauckman, Edward Haller, Nicholas Taran, Stephanie Rockfield, Abigail Ruiz-Rivera, Meera Nanjundan
The role of iron in the development of cancer remains unclear. We previously reported that iron reduces cell survival in a Ras/mitogen-activated protein kinase (MAPK)-dependent manner in ovarian cells; however, the underlying downstream pathway leading to reduced survival was unclear. Although levels of intracellular iron, ferritin/CD71 protein and reactive oxygen species did not correlate with iron-induced cell survival changes, we identified mitochondrial damage (via TEM) and reduced expression of outer mitochondrial membrane proteins (translocase of outer membrane: TOM20 and TOM70) in cell lines sensitive to iron...
March 1, 2015: Biochemical Journal
Bo Wei, Ye Cui, Yuefeng Huang, Heng Liu, Lin Li, Mi Li, Kang-Cheng Ruan, Qin Zhou, Chen Wang
UNLABELLED: Virus infection triggers immediate innate immune responses. Apoptosis represents another effective means to restrict virus invasion, besides robust expression of host cytokines and chemokines. IRF3 was recently demonstrated to be indispensable for Sendai virus (SeV)-induced apoptosis, but the underlying mechanism is not fully understood. Here we report that a dynamic protein complex, Tom70/Hsp90/IRF3/Bax, mediates SeV-induced apoptosis. The cytosolic proapoptotic protein Bax interacts specifically with IRF3 upon virus infection...
April 2015: Journal of Virology
Diane C Munday, Gareth Howell, John N Barr, Julian A Hiscox
OBJECTIVES: The aim of this study was to quantitatively characterise the mitochondrial proteome of airway epithelial cells infected with human respiratory syncytial virus (HRSV), a major cause of paediatric illness. METHODS: Quantitative proteomics, underpinned by stable isotope labelling with amino acids in cell culture, coupled to LC-MS/MS, was applied to mitochondrial fractions prepared from HRSV-infected and mock-infected cells 12 and 24 h post-infection. Datasets were analysed using ingenuity pathway analysis, and the results were validated and characterised using bioimaging, targeted inhibition and gene depletion...
March 2015: Journal of Pharmacy and Pharmacology
Kahori Shiba-Fukushima, Taku Arano, Gen Matsumoto, Tsuyoshi Inoshita, Shigeharu Yoshida, Yasushi Ishihama, Kwon-Yul Ryu, Nobuyuki Nukina, Nobutaka Hattori, Yuzuru Imai
The kinase PINK1 and the E3 ubiquitin (Ub) ligase Parkin participate in mitochondrial quality control. The phosphorylation of Ser65 in Parkin's ubiquitin-like (UBl) domain by PINK1 stimulates Parkin activation and translocation to damaged mitochondria, which induces mitophagy generating polyUb chain. However, Parkin Ser65 phosphorylation is insufficient for Parkin mitochondrial translocation. Here we report that Ser65 in polyUb chain is also phosphorylated by PINK1, and that phosphorylated polyUb chain on mitochondria tethers Parkin at mitochondria...
December 2014: PLoS Genetics
Jun Li, Man Qi, Changming Li, Dan Shi, Dasheng Zhang, Duanyang Xie, Tianyou Yuan, Jing Feng, Yi Liu, Dandan Liang, Xinran Xu, Jinjin Chen, Liang Xu, Hong Zhang, Jiangchuan Ye, Fei Lv, Jian Huang, Luying Peng, Yi-Han Chen
Pathological cardiac hypertrophy is an inevitable forerunner of heart failure. Regardless of the etiology of cardiac hypertrophy, cardiomyocyte mitochondrial alterations are always observed in this context. The translocases of mitochondrial outer membrane (Tom) complex governs the import of mitochondrial precursor proteins to maintain mitochondrial function under pathophysiological conditions; however, its role in the development of pathological cardiac hypertrophy remains unclear. Here, we showed that Tom70 was downregulated in pathological hypertrophic hearts from humans and experimental animals...
August 2014: Cell Research
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