We are analyzing https://link.springer.com/article/10.1007/s00018-012-1066-6.

Title:
Regulation of mitochondrial dynamics: convergences and divergences between yeast and vertebrates | Cellular and Molecular Life Sciences
Description:
In eukaryotic cells, the shape of mitochondria can be tuned to various physiological conditions by a balance of fusion and fission processes termed mitochondrial dynamics. Mitochondrial dynamics controls not only the morphology but also the function of mitochondria, and therefore is crucial in many aspects of a cell’s life. Consequently, dysfunction of mitochondrial dynamics has been implicated in a variety of human diseases including cancer. Several proteins important for mitochondrial fusion and fission have been discovered over the past decade. However, there is emerging evidence that there are as yet unidentified proteins important for these processes and that the fusion/fission machinery is not completely conserved between yeast and vertebrates. The recent characterization of several mammalian proteins important for the process that were not conserved in yeast, may indicate that the molecular mechanisms regulating and controlling the morphology and function of mitochondria are more elaborate and complex in vertebrates. This difference could possibly be a consequence of different needs in the different cell types of multicellular organisms. Here, we review recent advances in the field of mitochondrial dynamics. We highlight and discuss the mechanisms regulating recruitment of cytosolic Drp1 to the mitochondrial outer membrane by Fis1, Mff, and MIEF1 in mammals and the divergences in regulation of mitochondrial dynamics between yeast and vertebrates.
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Keywords {🔍}

mitochondrial, article, google, scholar, cas, pubmed, fission, yeast, drp, mitochondria, fusion, cell, protein, membrane, dynamics, cells, proteins, biol, mfn, dnmp, outer, human, mief, hfis, mammals, fisp, mdvp, required, opa, mammalian, machinery, mff, gtpase, morphology, parkin, cancer, recruitment, regulation, involved, mgmp, structures, role, domain, conserved, fzop, mol, fis, fragmentation, surface, function,

Topics {✒️}

skp1-cul1-f-box protein charcot-marie-tooth disease double membrane-bound organelles leucine zipper/ef hand n-terminal region facing large-scale cdna sequencing rhomboid-type protease pcp1 c-terminal hr2 region multi-step process requiring phosphatidylinositol 3-kinase-dependent protein c-terminal kinase domain m-aaa protease isoenzymes fundamental fission/fusion machineries dynamin-related protein drp-1 stress-induced mitochondrial hyperfusion article download pdf dimeric dnm1-g385d interacts central coiled-coil domain intramitochondrial dynamin-related gtpase c-terminal transmembrane domain c-terminal wd repeat rhomboid-related serine protease hypoxia-mediated mitochondrial fission hypoxia-triggered mitochondrial fission sh-sy5y cell lines n-terminal part exposed metalloprotease-mediated opa1 processing mediating gtp-dependent tethering mitochondrial fission-promoting protein n-terminal gtpase domain n-terminal transmembrane domain outer membrane-anchored proteins mitochondrial dynamin-related protein key dynamin-related gtpases phosphorylation-deficient drp1s637a mutant rhomboid-related protease presenilin modulate calcineurin-mediated dephosphorylation n-terminal tail mitochondrial fission/fusion machineries ubiquitin-proteasome-dependent degradation key fission-promoting proteins drp1-mediated mitochondrial fission mitochondrial fission/fusion machinery mitochondrial fusion/fission machinery f-box protein required drp1-dependent mitochondrial fission fusion-promoting factor mfn2 drp1-mediated fission process dynamin-related protein drp1 mitochondria-shaping proteins impact

Questions {❓}

Gogvadze V, Orrenius S, Zhivotovsky B (2008) Mitochondria in cancer cells: what is so special about them?
Zorzano A, Pich S (2006) What is the biological significance of the two mitofusin proteins present in the outer mitochondrial membrane of mammalian cells?

Schema {🗺️}

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      name:Department of Oncology-Pathology, Karolinska Institutet, CCK R8:05, Karolinska University Hospital Solna, Stockholm, Sweden

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