Peroxisome‐mitochondria interplay and disease

Schrader, Michael; Costello, Joseph L.; Godinho, Luís F.; Islinger, Markus

doi:10.1007/s10545-015-9819-7

Cited by 163 publications

(166 citation statements)

References 229 publications

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“…41 Functionally, these organelles cooperate in the regulation of the lipid and Reactive Oxigen Species homeostasis. At the structural level, mitochondria and peroxisomes share both molecular mechanisms and regulatory proteins for undergoing division.…”

Section: Discussionmentioning

confidence: 99%

Dysfunctional mitochondrial fission impairs cell reprogramming

et al. 2016

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We have recently shown that mitochondrial fission is induced early in reprogramming in a Drp1-dependent manner; however, the identity of the factors controlling Drp1 recruitment to mitochondria was unexplored. To investigate this, we used a panel of RNAi targeting factors involved in the regulation of mitochondrial dynamics and we observed that MiD51, Gdap1 and, to a lesser extent, Mff were found to play key roles in this process. Cells derived from Gdap1-null mice were used to further explore the role of this factor in cell reprogramming. Microarray data revealed a prominent down-regulation of cell cycle pathways in Gdap1-null cells early in reprogramming and cell cycle profiling uncovered a G2/M growth arrest in Gdap1-null cells undergoing reprogramming. High-Content analysis showed that this growth arrest was DNA damage-independent. We propose that lack of efficient mitochondrial fission impairs cell reprogramming by interfering with cell cycle progression in a DNA damage-independent manner.

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Section: Discussionmentioning

confidence: 99%

Dysfunctional mitochondrial fission impairs cell reprogramming

et al. 2016

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“…As a result of this tail-anchored (TA) topology, these proteins are post-translationally directed to their target membranes. Interestingly, numerous TA proteins are dually targeted to both peroxisomes and mitochondria [23]. This targeting appears to be largely dependent on the biochemical properties of their C-terminal amino acid sequence (principally the hydrophobicity of the TMD and the net charge in the tail region) and, as such, it can be characterized and used to predict the targeting of TA proteins [12].…”

Section: Targeting and Pex19 Bindingmentioning

confidence: 99%

Miro1 – the missing link to peroxisome motility

Castro

Schrader

2018

Communicative & Integrative Biology

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Peroxisomes are ubiquitous, highly dynamic, multifunctional compartments in eukaryotic cells, which perform key roles in cellular lipid metabolism and redox balance. Like other membrane-bound organelles, peroxisomes must move in the cellular landscape to perform localized functions, interact with other organelles and to properly distribute during cell division. However, our current knowledge of peroxisome motility in mammalian cells is still very limited. Recently, three independent studies have identified Miro1 as a regulator of peroxisome motility in mammalian cells. In these studies, the authors show that Miro1 is targeted to peroxisomes in several cell lines, in a process that relies on its interaction with the peroxisomal chaperone Pex19. Interestingly, however, different conclusions are drawn about which Miro1 isoforms are targeted to peroxisomes, how it interacts with Pex19 and most importantly, the type of motility Miro1 is regulating.

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“…1). This characteristic peroxisomal morphology was later observed in patient fibroblasts and led to the discovery of DRP1 deficiency, the first member of a new group of disorders with defects in peroxisomal and mitochondrial division (9,10).…”

Section: Introductionmentioning

confidence: 90%