scholarly journals Myc Stimulates Nuclearly Encoded Mitochondrial Genes and Mitochondrial Biogenesis

2005 ◽  
Vol 25 (14) ◽  
pp. 6225-6234 ◽  
Author(s):  
Feng Li ◽  
Yunyue Wang ◽  
Karen I. Zeller ◽  
James J. Potter ◽  
Diane R. Wonsey ◽  
...  
Keyword(s):  
Mitochondrial Biogenesis ◽  
Structure And Function ◽  
Wild Type ◽  
Primary Hepatocytes ◽  
Mitochondrial Mass ◽  
Mitochondrial Structure ◽  
Direct Binding ◽  
Rat Fibroblasts ◽  
And Function

ABSTRACT Although several genes involved in mitochondrial function are direct Myc targets, the role of Myc in mitochondrial biogenesis has not been directly established. We determined the effects of ectopic Myc expression or the loss of Myc on mitochondrial biogenesis. Induction of Myc in P493-6 cells resulted in increased oxygen consumption and mitochondrial mass and function. Conversely, compared to wild-type Myc fibroblasts, Myc null rat fibroblasts have diminished mitochondrial mass and decreased number of normal mitochondria. Reconstitution of Myc expression in Myc null fibroblasts partially restored mitochondrial mass and function and normal-appearing mitochondria. Concordantly, we also observed in primary hepatocytes that acute deletion of floxed murine Myc by Cre recombinase resulted in diminished mitochondrial mass in primary hepatocytes. Our microarray analysis of genes responsive to Myc in human P493-6 B lymphocytes supports a role for Myc in mitochondrial biogenesis, since genes involved in mitochondrial structure and function are overrepresented among the Myc-induced genes. In addition to the known direct binding of Myc to many genes involved in mitochondrial structure and function, we found that Myc binds the TFAM gene, which encodes a key transcriptional regulator and mitochondrial DNA replication factor, both in P493-6 lymphocytes with high ectopic MYC expression and in serum-stimulated primary human 2091 fibroblasts with induced endogenous MYC. These observations support a pivotal role for Myc in regulating mitochondrial biogenesis.

scholarly journals Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease

Life ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 82
Author(s):  
Veronika Kotrasová ◽  
Barbora Keresztesová ◽  
Gabriela Ondrovičová ◽  
Jacob A. Bauer ◽  
Henrieta Havalová ◽  
...  
Keyword(s):  
Mitochondrial Biogenesis ◽  
Mitochondrial Protein ◽  
Structure And Function ◽  
Stress Factors ◽  
Mitochondrial Proteins ◽  
Post Translational Modification ◽  
Mitochondrial Structure ◽  
Health And Disease ◽  
And Function

The major role of mitochondria is to provide cells with energy, but no less important are their roles in responding to various stress factors and the metabolic changes and pathological processes that might occur inside and outside the cells. The post-translational modification of proteins is a fast and efficient way for cells to adapt to ever changing conditions. Phosphorylation is a post-translational modification that signals these changes and propagates these signals throughout the whole cell, but it also changes the structure, function and interaction of individual proteins. In this review, we summarize the influence of kinases, the proteins responsible for phosphorylation, on mitochondrial biogenesis under various cellular conditions. We focus on their role in keeping mitochondria fully functional in healthy cells and also on the changes in mitochondrial structure and function that occur in pathological processes arising from the phosphorylation of mitochondrial proteins.

scholarly journals The role of nonbilayer phospholipids in mitochondrial structure and function

FEBS Letters ◽  
2017 ◽  
Vol 592 (8) ◽  
pp. 1273-1290 ◽  
Author(s):  
Writoban Basu Ball ◽  
John K. Neff ◽  
Vishal M. Gohil
Keyword(s):  
Structure And Function ◽  
Mitochondrial Structure ◽  
And Function

scholarly journals Drosophila MICOS knockdown impairs mitochondrial structure and function and promotes mitophagy in muscle tissue

Biology Open ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. bio054262
Author(s):  
Li-jie Wang ◽  
Tian Hsu ◽  
Hsiang-ling Lin ◽  
Chi-yu Fu
Keyword(s):  
Muscle Tissue ◽  
Mammalian Cells ◽  
Structure And Function ◽  
Tissue Homeostasis ◽  
Mitochondrial Morphology ◽  
Mitochondrial Structure ◽  
And Function ◽  
Nucleoid Structure

ABSTRACTThe mitochondrial contact site and cristae organizing system (MICOS) is a multi-protein interaction hub that helps define mitochondrial ultrastructure. While the functional importance of MICOS is mostly characterized in yeast and mammalian cells in culture, the contributions of MICOS to tissue homeostasis in vivo remain further elucidation. In this study, we examined how knocking down expression of Drosophila MICOS genes affects mitochondrial function and muscle tissue homeostasis. We found that CG5903/MIC26-MIC27 colocalizes and functions with Mitofilin/MIC60 and QIL1/MIC13 as a Drosophila MICOS component; knocking down expression of any of these three genes predictably altered mitochondrial morphology, causing loss of cristae junctions, and disruption of cristae packing. Furthermore, the knockdown flies exhibited low mitochondrial membrane potential, fusion/fission imbalances, increased mitophagy, and limited cell death. Reductions in climbing ability indicated deficits in muscle function. Knocking down MICOS genes also caused reduced mtDNA content and fragmented mitochondrial nucleoid structure in Drosophila. Together, our data demonstrate an essential role of Drosophila MICOS in maintaining proper homeostasis of mitochondrial structure and function to promote the function of muscle tissue.

scholarly journals Molecular Dynamics of SARS-CoV-2 Nsp1 Structural Changes Associated with Variant Mutations

2021 ◽  
Author(s):  
Shokouh Rezaei ◽  
Yahya Sefidbakht ◽  
Filipe Pereira
Keyword(s):  
Molecular Dynamics ◽  
Conformational Changes ◽  
Structural Changes ◽  
Structure And Function ◽  
Dynamics Simulation ◽  
Structural Protein ◽  
Wild Type ◽  
Deletion Mutations ◽  
And Function

Abstract SARS-CoV-2 non-structural protein 1 (Nsp1) is a virulence factor that inhibits the translation of host mRNAs and interact with viral RNA. Despite the relevance of Nsp1, few studies have been conducted to understand the effect of mutations on Nsp1 structure and function. Here, we provide a molecular dynamics simulation of SARS-CoV-2 Nsp1, wild type and variants. We found that SARS-CoV-2 Nsp1 has a more Rg value than SARS-CoV-1 Nsp1, with indicate an effect on the folding protein. This result suggest that SARS-CoV-2 Nsp1 can more easily approach the active site of the ribosome compared to SARS-CoV-1 Nsp1. In addition, we found that the C-terminal of the SARS-CoV-2 Nsp1, in particular residues 164 to 170, are more flexible than other regions of SARS-CoV-2 Nsp1 and SARS-CoV-1 Nsp1, confirming the role of this region in the interaction with the 40S subunit. Moreover, multiple deletion mutations have been found in the N/C-terminal of the SARS-CoV-2 Nsp1, which seems the effect of SARS-CoV-2 Nsp1 multiple deletions is greater than that of substitutions. Among all deletions, D156-158 and D80-90 may destabilize the protein structure and possibly increase the virulence of the SARS-CoV-2. Overall, our findings reinforce the importance of studying Nsp1 conformational changes in new variants and its effect on virulence of SARS-CoV-2.

The role of recovery of mitochondrial structure and function in desiccation tolerance of pea seeds

2011 ◽  
Vol 144 (1) ◽  
pp. 20-34 ◽  
Author(s):  
Wei-Qing Wang ◽  
Hong-Yan Cheng ◽  
Ian M. Møller ◽  
Song-Quan Song
Keyword(s):  
Desiccation Tolerance ◽  
Structure And Function ◽  
Mitochondrial Structure ◽  
Pea Seeds ◽  
And Function

scholarly journals Effect of ApoE isoforms on mitochondria in Alzheimer disease

Neurology ◽  
2020 ◽  
Vol 94 (23) ◽  
pp. e2404-e2411 ◽  
Author(s):  
Junxiang Yin ◽  
Eric M. Reiman ◽  
Thomas G. Beach ◽  
Geidy E. Serrano ◽  
Marwan N. Sabbagh ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Alzheimer Disease ◽  
Human Brain ◽  
Cognitive Performance ◽  
Mitochondrial Biogenesis ◽  
Mitochondrial Dynamics ◽  
Structure And Function ◽  
Mitochondrial Structure ◽  
Apoe Isoforms ◽  
And Function

ObjectiveTo test the hypothesis that ApoE isoforms affect mitochondrial structure and function that are related to cognitive impairment in Alzheimer disease (AD), we systematically investigated the effects of ApoE isoforms on mitochondrial biogenesis and dynamics, oxidative stress, synapses, and cognitive performance in AD.MethodsWe obtained postmortem human brain tissues and measured proteins that are responsible for mitochondrial biogenesis (peroxisome proliferator-activated receptor-gamma coactivator-1α [PGC-1α] and sirtuin 3 [SIRT3]), for mitochondrial dynamics (mitofusin 1 [MFN1], mitofusin 2 [MFN2], and dynamin-like protein 1 [DLP1]), for oxidative stress (superoxide dismutase 2 [SOD2] and forkhead-box protein O3a [Foxo3a]), and for synapses (postsynaptic density protein 95 [PSD95] and synapsin1 [Syn1]). A total of 46 cases were enrolled, including ApoE-ɛ4 carriers (n = 21) and noncarriers (n = 25).ResultsLevels of these proteins were compared between ApoE-ɛ4 carriers and noncarriers. ApoE-ɛ4 was associated with impaired mitochondrial structure and function, oxidative stress, and synaptic integrity in the human brain. Correlation analysis revealed that mitochondrial proteins and the synaptic protein were strongly associated with cognitive performance.ConclusionApoE isoforms influence mitochondrial structure and function, which likely leads to alteration in oxidative stress, synapses, and cognitive function. These mitochondria-related proteins may be a harbinger of cognitive decline in ApoE-ɛ4 carriers and provide novel therapeutic targets for prevention and treatment of AD.

scholarly journals Nuclear mutations affecting mitochondrial structure and function in Chlamydomonas.

1977 ◽  
Vol 73 (1) ◽  
pp. 56-77 ◽  
Author(s):  
A Wiseman ◽  
N W Gillham ◽  
J E Boynton
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Structure And Function ◽  
Class Iii ◽  
Wild Type ◽  
Mitochondrial Ultrastructure ◽  
Cytochrome Oxidase Activity ◽  
Mitochondrial Structure ◽  
Nadh Cytochrome ◽  
And Function

Wild type cells of the green alga Chlamydomonas reinhardtii can grow in the in the dark by taking up and respiring exogenously supplied acetate. Obligate photoautotrophic (dark dier, dk) mutants of this alga have been selected which grow at near wild type rates in the light, but rapidly die when transferred to darkness because of defects in mitochondrial structure and function. In crosses of the dk mutants to wild type, the majority of the mutants are inherited in a mendelian fashion, although two have been isolated which are inherited in a clearly nonmendelian fashion. Nine mendelian dk mutants have been analyzed in detail, and belong to eight different complementation groups representing eight gene loci. These mutants have been tentatively grouped into three classes on the basis of the pleiotropic nature of their phenotypic defects. Mutants in Class I have gross alterations in the ultrastructure of their mitochondrial inner membranes together with deficiencies in cytochrome oxidase and antimycin/rotenone-sensitive NADH-cytochrome c reductase activities. Mutants in Class II have a variety of less severe alterations in mitochondrial ultrastructure and deficiencies in cytochrome oxidase activity. Mutants in Class III have normal or near normal mitochondrial ultrastructure and reduced cytochrome oxidase activity. Eight of the nine mutants show corresponding reductions in cyanide-sensitive respiration.

Sign in / Sign up

Export Citation Format

Share Document