Mitochondrial dynamics: Biological roles, molecular machinery, and related diseases

El‐Hattab, Ayman W.; Suleiman, Jehan; Almannai, Mohammed; Scaglia, Fernando

doi:10.1016/j.ymgme.2018.10.003

Cited by 112 publications

(100 citation statements)

References 43 publications

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“…Mitochondria morphology, distribution and function are dependent on the balanced regulation of mitochondrial fusion and fission (El-Hattab et al, 2018). The striking increase in the amount of mitochondria and their elongated appearance, suggest that excessive mitochondrial fission may occur in Ptbp2 cKO spermatids.…”

Section: Ptbp2-deletion Alters Mitochondrial Dynamics In Spermatidsmentioning

confidence: 99%

PTBP2-dependent alternative splicing regulates protein transport and mitochondria morphology in post-meiotic germ cells.

Hannigan

Fujioka

Brett-Morris

et al. 2018

Preprint

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The RNA binding protein PTBP2 (polypyrimidine tract binding protein 2) is a key regulator of tissue-specific alternative RNA splicing. In the testis, PTBP2 is expressed in meiotic and post-meiotic germ cells (spermatocytes and spermatids, respectively). In these cells, PTBP2 is required for proper alternative mRNA splicing for over 200 genes, disproportionately affecting genes encoding proteins involved in protein trafficking via transport vesicles. In this study, we used electron microscopy to test the hypothesis that protein trafficking is impaired in the absence of PTBP2, and to further investigate why spermatogenesis abruptly ceases in PTBP2-deficienct spermatids. Ultrastructural analysis shows that protein trafficking in spermatids is aberrant in the absence of PTBP2. Unexpectedly, we also found that mitochondria morphology and number are significantly altered in PTBP2-deficient spermatids, consistent with increased mitochondria fission. Furthermore, we show that genes with key roles in mitochondria dynamics and function are post-transcriptionally regulated by PTBP2 and in different stages of spermatogenesis. Collectively, the data provide ultrastructural evidence that alternative splicing regulation by PTBP2 during spermatogenesis is critical for proper regulation of protein trafficking and mitochondria morphology.

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Section: Ptbp2-deletion Alters Mitochondrial Dynamics In Spermatidsmentioning

confidence: 99%

PTBP2-dependent alternative splicing regulates protein transport and mitochondria morphology in post-meiotic germ cells.

Hannigan

Fujioka

Brett-Morris

et al. 2018

Preprint

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“…The OMM is smooth and highly permeable to most solutes, whereas the IMM is impermeable. Besides, the IMM is folded into cristae, allowing to increase the sur-face of this membrane (El-Hattab et al 2018). Mitochondria form unconnected, functionally distinct entities (Collins et al 2002) and their number varies from tens (in lymphocytes [Potter and Ward 1942]) to thousands (in hepatocytes) per cell (Weibel et al 1969).…”

mentioning

confidence: 99%

Cytoplasmic and Mitochondrial Calcium Signaling: A Two-Way Relationship

Wacquier

Combettes

Dupont

2019

Cold Spring Harb Perspect Biol

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Intracellular Ca 2+ signals are well organized in all cell types, and trigger a variety of vital physiological processes. The temporal and spatial characteristics of cytosolic Ca 2+ increases are mainly governed by the fluxes of this ion across the membrane of the endoplasmic/sarcoplasmic reticulum and the plasma membrane. However, various Ca 2+ transporters also allow for Ca 2+ exchanges between the cytoplasm and mitochondria. Increases in mitochondrial Ca 2+ stimulate the production of ATP, which allows the cells to cope with the increased energy demand created by the stimulus. Less widely appreciated is the fact that Ca 2+ handling by mitochondria also shapes cytosolic Ca 2+ signals. Indeed, the frequency, amplitude, and duration of cytosolic Ca 2+ increases can be altered by modifying the rates of Ca 2+ transport into, or from, mitochondria. In this review, we focus on the interplay between mitochondria and Ca 2+ signaling, highlighting not only the consequences of cytosolic Ca 2+ changes on mitochondrial Ca 2+ , but also how cytosolic Ca 2+ dynamics is controlled by modifications of the Ca 2+ -handling properties and the metabolism of mitochondria.

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“…Tethering thus increases the processivity of kinesin-1, to enable microtubule-based transport in the crowded cytoplasmic environment. We propose tethering by auxiliary proteins as a 13 general mechanism regulating molecular motors and other filament-associated proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Mitochondrial trafficking between stroma and cancer cells is relevant in tumour initiation and progression 3,8,9 and dysfunctions in the distribution of mitochondria are connected with neurodegenerative diseases, including Alzheimer's disease, Huntington's disease or amyotrophic lateral sclerosis [10][11][12][13][14][15] .…”

Section: Introductionmentioning

confidence: 99%

Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments

Henrichs

Grycová

Bařinka

et al. 2020

Preprint

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Intracellular trafficking of organelles, driven by kinesin-1 stepping along microtubules, underpins essential processes including neuronal activity. In absence of other proteins on the microtubule surface, kinesin-1 performs micron-long runs. Under protein crowding conditions, however, kinesin-1 motility is drastically impeded. It is thus unclear how kinesin-1 acts as an efficient transporter in crowded intracellular environments. Here, we demonstrate that TRAK1 (Milton), an adaptor protein essential for mitochondrial trafficking, activates kinesin-1 and increases its robustness of stepping in protein crowding conditions. Interaction with TRAK1 i) facilitated kinesin-1 navigation around obstacles, ii) increased the probability of kinesin-1 passing through cohesive envelopes of tau and iii) increased the run length of kinesin-1 in cell lysate.We explain the enhanced motility by the observed direct interaction of TRAK1 with microtubules, providing an additional anchor for the kinesin-1-TRAK1 complex. We propose adaptor-mediated tethering as a mechanism regulating kinesin-1 motility in various cellular environments.

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Mitochondrial dynamics: Biological roles, molecular machinery, and related diseases

Cited by 112 publications

References 43 publications

PTBP2-dependent alternative splicing regulates protein transport and mitochondria morphology in post-meiotic germ cells.

PTBP2-dependent alternative splicing regulates protein transport and mitochondria morphology in post-meiotic germ cells.

Cytoplasmic and Mitochondrial Calcium Signaling: A Two-Way Relationship

Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments

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