Mitochondrial-cytoskeletal interactions: dynamic associations that facilitate network function and remodeling

Moore, Andrew S.; Holzbaur, Erika L.F.

doi:10.1016/j.cophys.2018.03.003

Cited by 70 publications

(57 citation statements)

References 50 publications

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“…Besides the ER, the actin cytoskeleton is also involved in regulating mitochondrial fission (40,132). The cycling of actin assembly and disassembly around mitochondrial subpopulations efficiently promotes local Drp1-dependent mitochondrial fission.…”

Section: Roles Of the Actin Cytoskeleton In Mitochondrial Dynamicsmentioning

confidence: 99%

“…The ER and the actin cytoskeleton have been reported to be involved in mitochondrial dynamics in cooperation with Drp1 (129,132,134), but whether the ER and actin cytoskeleton play a role in Drp1-independent fission is unknown. Emerging evidence, however, suggests that F-actin depolymerization significantly prevents hFis1 overexpressioninduced mitochondrial fragmentation in a Drp1-independent manner, implying that the actin cytoskeleton plays a Drp1independent role in regulating mitochondrial fission (88).…”

Section: Drp1-independent Mitochondrial Fission Pathways In Mammalsmentioning

confidence: 99%

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Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges

et al. 2020

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Mitochondria are highly dynamic organelles and important for a variety of cellular functions. They constantly undergo fission and fusion events, referred to as mitochondrial dynamics, which affects the shape, size, and number of mitochondria in the cell, as well as mitochondrial subcellular transport, mitochondrial quality control (mitophagy), and programmed cell death (apoptosis). Dysfunctional mitochondrial dynamics is associated with various human diseases. Mitochondrial dynamics is mediated by a set of mitochondria-shaping proteins in both yeast and mammals. In this review, we describe recent insights into the potential molecular mechanisms underlying mitochondrial fusion and fission, particularly highlighting the coordinating roles of different mitochondria-shaping proteins in the processes, as well as the roles of the endoplasmic reticulum (ER), the actin cytoskeleton and membrane phospholipids in the regulation of mitochondrial dynamics. We particularly focus on emerging roles for the mammalian mitochondrial proteins Fis1, Mff, and MIEFs (MIEF1 and MIEF2) in regulating the recruitment of the cytosolic Drp1 to the surface of mitochondria and how these proteins, especially Fis1, mediate crosstalk between the mitochondrial fission and fusion machineries. In summary, this review provides novel insights into the molecular mechanisms of mammalian mitochondrial dynamics and the involvement of these mechanisms in apoptosis and autophagy.

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Section: Roles Of the Actin Cytoskeleton In Mitochondrial Dynamicsmentioning

confidence: 99%

Section: Drp1-independent Mitochondrial Fission Pathways In Mammalsmentioning

confidence: 99%

Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges

et al. 2020

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“…39 Since (a) cytoskeletal dynamics have an important role in autophagy, 40 (b) mitochondria interact with the cytoskeletal components, 21 (c) mitophagy is regulated by cytoskeletal components, 41 and (d) microgravity rapidly and steadily disassembles HUVEC cytoskeleton, 3,7,8,10 we anticipate that a link might exist between autophagy, mitochondria content, and cytoskeletal remodeling in our experimental model. 39 Since (a) cytoskeletal dynamics have an important role in autophagy, 40 (b) mitochondria interact with the cytoskeletal components, 21 (c) mitophagy is regulated by cytoskeletal components, 41 and (d) microgravity rapidly and steadily disassembles HUVEC cytoskeleton, 3,7,8,10 we anticipate that a link might exist between autophagy, mitochondria content, and cytoskeletal remodeling in our experimental model.…”

Section: Discussionmentioning

confidence: 99%

“…19 Different stimuli are able to modulate mitochondrial content and function. 21 Because research in space is limited by the high costs and low flight opportunities, several ground-based tools have been developed for simulating microgravity on Earth, 22 all based on eliminating a preferential direction of the gravity vector by continuous rotation. 20 Mitochondrial dynamics is strictly linked to cytoskeletal organization, which has a relevant role in maintaining mitochondrial network and function.…”

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confidence: 99%

Mitophagy contributes to endothelial adaptation to simulated microgravity

et al. 2019

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Exposure to real or simulated microgravity is sensed as a stress by mammalian cells, which activate a complex adaptive response. In human primary endothelial cells, we have recently shown the sequential intervention of various stress proteins which are crucial to prevent apoptosis and maintain cell function. We here demonstrate that mitophagy contributes to endothelial adaptation to gravitational unloading. After 4 and 10 d of exposure to simulated microgravity in the rotating wall vessel, the amount of BCL2 interacting protein 3, a marker of mitophagy, is increased and, in parallel, mitochondrial content, oxygen consumption, and maximal respiratory capacity are reduced, suggesting the acquisition of a thrifty phenotype to meet the novel metabolic challenges generated by gravitational unloading. Moreover, we suggest that microgravity induced‐disorganization of the actin cytoskeleton triggers mitophagy, thus creating a connection between cytoskeletal dynamics and mitochondrial content upon gravitational unloading.

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“…Importantly for the present study, mitochondria can interact with the cytoskeleton such that mitochondria serve as an energy source that can facilitate cytoskeletal remodeling, while the cytoskeleton itself can regulate changes in mitochondrial dynamics [26,27]. Interplay between these organelles can thus regulate cellular energy availability, intracellular transport, and cell motility [28,29].…”

Section: Wnt5a Modulates Mitochondrial-cytoskeletal Colocalization VImentioning

confidence: 90%

Wnt5a regulates Ameloblastoma Cell Migration by modulating Mitochondrial and Cytoskeletal Dynamics

Qin¹,

Niu²,

Shi

et al. 2020

J. Cancer

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Objective: Abnormal expression of Wnt5a has been detected in various tumors, including ameloblastoma (AB). Yet, there is no specific mechanistic evidence for the functional role of Wnt5a in AB. In this study, we aimed to conduct a mechanistic examination of the importance of Wnt5a in AB development. Methods: The expressions of Wnt5a and Coro1A were examined by Western blot and immunohistochemistry both in AB tissues and AM-1 cells. The number and size of mitochondria were detected by electronic transmission microscope and confocal microscope. Gain-of-function and loss-of-function assays were used to explore the biological roles of Wnt5a and Coro1A in organelle dynamics changes and cell migration. Cell migration was detected by wound healing and transwell assay. Results: We found that in AM-1 cells, up-regulation of Wnt5a led to enhanced mitochondrial energy production and altered calcium homeostasis, with elevated calcium levels directly leading to altered mitochondrial dynamics and interactions between the cytoskeleton and the mitochondria. When Wnt5a or its downstream cytoskeleton-associated protein Coro1A was knocked down, the migration capacity of AM-1 cells was markedly impaired. Conclusion: Together, these results suggest that Wnt5a plays mitochondria and cytoskeleton specific roles in regulating the development of human AB, with its down-regulation leading to impaired tumor development, thus highlighting Wnt5a or Coro1A as potentially viable therapeutic targets for the treatment of AB.

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Mitochondrial-cytoskeletal interactions: dynamic associations that facilitate network function and remodeling

Cited by 70 publications

References 50 publications

Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges

Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges

Mitophagy contributes to endothelial adaptation to simulated microgravity

Wnt5a regulates Ameloblastoma Cell Migration by modulating Mitochondrial and Cytoskeletal Dynamics

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