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Mitochondrial Biology and Reactive Oxygen Species

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (20 April 2025) | Viewed by 1696

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Laboratory of Mitochondrial Biochemistry, Department of Bioenergetics, Faculty of Biology, Adam Mickiewicz University, 61-614 Poznan, Poland
Interests: amp-activated protein kinase; ampk; mtorc1; mitochondrial biogenesis; mitochondrial phosphoproteome; phosphoproteomics; dictyostelium discoideum
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Special Issue Information

Dear Colleagues,

Mitochondria are involved in many processes critical to cell function and dysfunction, including maintaining metabolic and ionic homeostasis, calcium signaling, cell differentiation and growth, cell cycle control and cell death. They are crucial for cellular energy production and the formation of reactive oxygen species (ROS). Mitochondrial coenzyme Q (mtQ) is also involved in mitochondrial reactive oxygen species (mtROS). The redox state of the mtQ pool is a central bioenergetic parameter that alters in response to changes in mitochondrial function. It reflects mitochondrial bioenergetic activity and mtROS formation level and thus the oxidative stress associated with the mitochondria. Under oxidative stress conditions, excessive mtROS production can lead to various oxidative damage, including oxidative modification of cellular macromolecules such as lipids, DNA and proteins, which is the cause of aging and many diseases. In addition, damaged mitochondria release apoptotic factors that act as signals that induce cell death.  In this Special Issue, we aim to gain new and evolving knowledge of mitochondrial biology. We welcome reviews and original research articles encompassing the role of mitochondria in the regulation of metabolic health, mtROS in mitochondrial stress response and metabolic regulation, expand our understanding of the mitochondrial stress response and how it can be leveraged to improve systemic metabolic health.

This Special Issue is supervised by Dr. Wieslawa Jarmuszkiewicz and assisted by our Topical Advisory Panel Member Dr. Lukasz Galganski (Adam Mickiewicz University).

Dr. Wieslawa Jarmuszkiewicz
Guest Editor

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Keywords

  • mitochondrial biology
  • mitochondrial dysfunction
  • mitochondrial coenzyme Q
  • metabolic homeostasis
  • oxidative stress
  • reactive oxygen species

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Published Papers (1 paper)

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Research

18 pages, 2224 KiB  
Communication
Distribution of the p66Shc Adaptor Protein Among Mitochondrial and Mitochondria—Associated Membranes Fractions in Normal and Oxidative Stress Conditions
by Magdalena Lebiedzinska-Arciszewska, Barbara Pakula, Massimo Bonora, Sonia Missiroli, Yaiza Potes, Patrycja Jakubek-Olszewska, Ines C. M. Simoes, Paolo Pinton and Mariusz R. Wieckowski
Int. J. Mol. Sci. 2024, 25(23), 12835; https://doi.org/10.3390/ijms252312835 - 29 Nov 2024
Cited by 1 | Viewed by 1128
Abstract
p66Shc is an adaptor protein and one of the cellular fate regulators since it modulates mitogenic signaling pathways, mitochondrial function, and reactive oxygen species (ROS) production. p66Shc is localized mostly in the cytosol and endoplasmic reticulum (ER); however, under oxidative stress, p66Shc is [...] Read more.
p66Shc is an adaptor protein and one of the cellular fate regulators since it modulates mitogenic signaling pathways, mitochondrial function, and reactive oxygen species (ROS) production. p66Shc is localized mostly in the cytosol and endoplasmic reticulum (ER); however, under oxidative stress, p66Shc is post-translationally modified and relocates to mitochondria. p66Shc was found in the intermembrane space, where it interacts with cytochrome c, contributing to the hydrogen peroxide generation by the mitochondrial respiratory chain. Our previous studies suggested that p66Shc is localized also in mitochondria-associated membranes (MAM). MAM fraction consists of mitochondria and mostly ER membranes. Contact sites between ER and mitochondria host proteins involved in multiple processes including calcium homeostasis, apoptosis, and autophagy regulation. Thus, p66Shc in MAM could participate in processes related to cell fate determination. Due to reports on various and conditional p66Shc intracellular localization, in the present paper, we describe the allocation of p66Shc pools in different subcellular compartments in mouse liver tissue and HepG2 cell culture. We provide additional evidence for p66Shc localization in MAM. In the present study, we use precisely purified subcellular fraction isolated by differential centrifugation-based protocol from control mouse liver tissue and HepG2 cells and from cells treated with hydrogen peroxide to promote mitochondrial p66Shc translocation. We performed controlled digestion of crude mitochondrial fraction, in which the degradation patterns of p66Shc and MAM fraction marker proteins were comparable. Moreover, we assessed the distribution of the individual ShcA isoforms (p46Shc, p52Shc, and p66Shc) in the subcellular fractions and their contribution to the total ShcA in control mice livers and HepG2 cells. In conclusion, we showed that a substantial pool of p66Shc protein resides in MAM in control conditions and after oxidative stress induction. Full article
(This article belongs to the Special Issue Mitochondrial Biology and Reactive Oxygen Species)
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