Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes.
By Koji Okamoto, J. Shaw. Annual Review of Genetics, 2005
763 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/996444ab3d78557892bb19493de2ee76e99ab4dc
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Citations in the corpus
- Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice (2009, background): “Mitochondrial morphology changes dynamically as a result of a balance in the fusion and fission occurring in response to cellular energy demands, differentiation or pathological condition”
- Fission and selective fusion govern mitochondrial segregation and elimination by autophagy (2008, background): “The role of fission in mitochondrial autophagy was evaluated in INS1 cells expressing low levels of FIS1, the rate-limiting protein in the mitochondrial fission process (Yoon et al, 2003; Okamoto and Shaw, 2005) and in cells expressing a dominant-negative form of the fission protein DRP1 (DRP1, or D”
- Mitochondrial dynamics–fusion, fission, movement, and mitophagy–in neurodegenerative diseases (2009, background): “This mitophagy is dependent on loss of fusion and the presence of fission, because OPA1overexpression, Fis1 RNAi, and Drp1 dominant-negative expression all reduce levels of mitophagy.”
- The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. (2008, background): “Mitochondrial fission facilitates the redistribution of mitochondria in response to local changes in the demand for ATP, whereas mitochondrial fusion is needed to exchange mitochondrial DNA and other components that may become damaged over time (Okamoto and Shaw, 2005; Chan, 2006).”
- OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L (2007, neutral): “Mitochondrial fusion plays an important role in controlling the shape and function of mitochondria (Okamoto and Shaw, 2005; Chan, 2006).”
- Dynamin, a membrane remodelling GTPase (2012, background): “The two intracellular fission reactions besides endocytosis that clearly require DLPs are the fission of mitochondri”
- Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells (2010, background): “mitochondrial networks, and this dynamic morphology is essential for normal mitochondrial and cellular functions (Karbowski and Youle, 2003; Okamoto and Shaw, 2005; Chan, 2006; McBride et al., 2006; Cerveny et al., 2007b; Hoppins et al., 2007; Benard and Karbowski, 2009).”
- Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. (2008, background): “Detailed reviews on the molecular machinery of mitochondrial fusion and fission, protein turnover and autophagy are available in the these references [8,31–36].”
- The role of mitochondria in apoptosis. (2008, background): “sion and fission rely on the function of multiple proteins that mediate the remodeling of the outer and inner mitochondrial membrane (75).”
- Mitochondrial fusion and fission in cell life and death (2010, background): “Although most of the evolutionarily conserved core components of the mitochondrial fusion and fission machineries have been described in the past 15 years ( Table 1 ), more recent work revealed mechanistic insights into their molecular functio”
- The pathways of mitophagy for quality control and clearance of mitochondria (2012, background): “Mitochondrial fission and fusion are regulated by members of a family of conserved large GTPases, initially identified in yeast.(50,51) The dynamin-like GTPase, dynain-related protein 1 (Drp1) (Dnm1 in yeast), mediates fission by forming a multimeric complex that wraps around the outer membrane of m”
- Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations (2010, neutral): “INTRODUCTION Mitochondrial fusion and fission have emerged as important processes that govern mitochondrial function from yeast to mammals (Detmer and Chan, 2007a; Suen et al., 2008; Okamoto and Shaw, 2005; Hoppins et al., 2007).”
- Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins (2008, neutral): “We next investigated effect of APP overexpression on mitochondrial fission (i.e., DLP1 and Fis1) and fusion proteins (i.e., OPA1, Mfn1, and Mfn2).”