The structure of rat liver mitochondria: A reevaluation

Brandt, Julie; Martin, A. J. P.; Lucas, Fred V.; Vorbeck, Marie L.

doi:10.1016/s0006-291x(74)80091-4

Cited by 39 publications

(13 citation statements)

References 3 publications

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“…Similarly, in leukocytes, mitochondrial fission is important for chemotactic activity (Campello et al, 2006). In contrast, tissues with high metabolic fluxes, such as skeletal muscle and liver, have large mitochondria upon differentiation (Bakeeva et al, 1981;Bakeeva et al, 1978;Brandt et al, 1974). Mitochondrial fusion is also indispensable for mouse embryonic development (Chen et al, 2003a) and Drosophila spermatogenesis (Hales and Fuller, 1997).…”

Section: Mitochondria Undergo Extensive Fusion During Ifm Developmentmentioning

confidence: 99%

Drosophila Erect wing (Ewg) controls mitochondrial fusion during muscle growth and maintenance by regulation of the Opa1-like gene

Rai

Katti

Nongthomba

2013

Journal of Cell Science

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Mitochondrial biogenesis and morphological changes are associated with tissue-specific functional demand, but the factors and pathways that regulate these processes have not been completely identified. A lack of mitochondrial fusion has been implicated in various developmental and pathological defects. The spatiotemporal regulation of mitochondrial fusion in a tissue such as muscle is not well understood. Here, we show in Drosophila indirect flight muscles (IFMs) that the nuclear-encoded mitochondrial inner membrane fusion gene, Opa1-like, is regulated in a spatiotemporal fashion by the transcription factor/co-activator Erect wing (Ewg). In IFMs null for Ewg, mitochondria undergo mitophagy and/or autophagy accompanied by reduced mitochondrial functioning and muscle degeneration. By following the dynamics of mitochondrial growth and shape in IFMs, we found that mitochondria grow extensively and fuse during late pupal development to form the large tubular mitochondria. Our evidence shows that Ewg expression during early IFM development is sufficient to upregulate Opa1-like, which itself is a requisite for both late pupal mitochondrial fusion and muscle maintenance. Concomitantly, by knocking down Opa1-like during early muscle development, we show that it is important for mitochondrial fusion, muscle differentiation and muscle organization. However, knocking down Opa1-like, after the expression window of Ewg did not cause mitochondrial or muscle defects. This study identifies a mechanism by which mitochondrial fusion is regulated spatiotemporally by Ewg through Opa1-like during IFM differentiation and growth.

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Section: Mitochondria Undergo Extensive Fusion During Ifm Developmentmentioning

confidence: 99%

Drosophila Erect wing (Ewg) controls mitochondrial fusion during muscle growth and maintenance by regulation of the Opa1-like gene

Rai

Katti

Nongthomba

2013

Journal of Cell Science

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“…Fusion of mitochondria apparently occurs developmentally in diaphragm muscle in the rat (Bakeeva et al, 1981), after mitosis in Euglena (Calvayrac et al 1974), before mitosis in scorpion (reviewed in Warren and Wicker, 1996), and after mating in Saccharomyces cerevisiae (Nunnari et al, 1997). The fusion of mitochondria in mammalian cells has been inferred from the extended filamentous morphology observed in a number of cell types (Johnson et al 1980) and tissues (Brandt et al, 1974;Kirkwood et al, 1986). A particularly well characterized mitochondrial fusion occurs in the developing Drosophila spermatid.…”

Section: S Isenmann Et Almentioning

confidence: 99%

A Splice-Isoform of Vesicle-associated Membrane Protein-1 (VAMP-1) Contains a Mitochondrial Targeting Signal

Isenmann

Khew‐Goodall

Gamble

et al. 1998

MBoC

122

119

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Screening of a library derived from primary human endothelial cells revealed a novel human isoform of vesicle-associated membrane protein-1 (VAMP-1), a protein involved in the targeting and/or fusion of transport vesicles to their target membrane. We have termed this novel isoform VAMP-1B and designated the previously described isoform VAMP-1A. VAMP-1B appears to be an alternatively spliced form of VAMP-1. A similar rat splice variant of VAMP-1 (also termed VAMP-1B) has recently been reported. Five different cultured cell lines, from different lineages, all contained VAMP-1B but little or no detectable VAMP-1A mRNA, as assessed by PCR. In contrast, brain mRNA contained VAMP-1A but no VAMP-1B. The VAMP-1B sequence encodes a protein identical to VAMP-1A except for the carboxy-terminal five amino acids. VAMP-1 is anchored in the vesicle membrane by a carboxy-terminal hydrophobic sequence. In VAMP-1A the hydrophobic anchor is followed by a single threonine, which is the carboxy-terminal amino acid. In VAMP-1B the predicted hydrophobic membrane anchor is shortened by four amino acids, and the hydrophobic sequence is immediately followed by three charged amino acids, arginine-arginine-aspartic acid. Transfection of human endothelial cells with epitope-tagged VAMP-1B demonstrated that VAMP-1B was targeted to mitochondria whereas VAMP-1A was localized to the plasma membrane and endosome-like structures. Analysis of C-terminal mutations of VAMP-1B demonstrated that mitochondrial targeting depends both on the addition of positive charge at the C terminus and a shortened hydrophobic membrane anchor. These data suggest that mitochondria may be integrated, at least at a mechanistic level, to the vesicular trafficking pathways that govern protein movement between other organelles of the cell.

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“…A chain of the long end-to-end-arranged mitochondria were observed in spermatozoa (for refs., see . In the liver cell, Brandt et al (1974) found mitochondria of two types, the small spherical and the large branched ones. A similar picture was revealed in ascites tumor cells and in an algal cell, Polytorna papillatum.…”

Section: Giant Mitochondria and Reticulum Mitochondrialementioning

confidence: 99%

Power transmission along biological membranes

Skulachev

1990

J. Membrain Biol.

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Hypothesis on long-distance power transmission along extended energy-transducing membranes (Skulachev, 1969, 1971, 1980), has been experimentally proven in four different systems, namely, (i) trichomes of filamentous cyanobacterium Phormidium uncinatum; (ii) filamentous mitochondria and mitochondrial network in fibroblasts; (iii) clusters of roundish heart muscle mitochondria interconnected with mitochondrial junctions; (iv) mixed animal cell cultures interconnected with gap junctions. In all cases, energy was shown to be transmitted in the form of a transmembrane electric potential difference. The transmission occurred for distances as long as several tens of micrometers. Since the (a) delta-muH-bearing cytoplasmic membrane of cyanobacteria and the inner mitochondrial membrane and (b) delta-muNa-bearing outer animal cell membrane were found to be competent in such an effect, one may assume that the power transmission is a fundamental function of extended membrane systems. This mechanism can be used at the intracellular level (mitochondrial) as well as at the supracellular level (cytoplasmic and outer cell membranes). Studies on the possible involvement of membranes in lateral transport of oxygen, ions, fatty acids and membrane proteins seem to hold good promise.

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The structure of rat liver mitochondria: A reevaluation

Cited by 39 publications

References 3 publications

Drosophila Erect wing (Ewg) controls mitochondrial fusion during muscle growth and maintenance by regulation of the Opa1-like gene

Drosophila Erect wing (Ewg) controls mitochondrial fusion during muscle growth and maintenance by regulation of the Opa1-like gene

A Splice-Isoform of Vesicle-associated Membrane Protein-1 (VAMP-1) Contains a Mitochondrial Targeting Signal

Power transmission along biological membranes

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