9 results match your criteria fzo1 turnover

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A AAA ATPase Cdc48 with a cofactor Ubx2 facilitates ubiquitylation of a mitochondrial fusion-promoting factor Fzo1 for proteasomal degradation.

J Biochem 2020 Mar;167(3):279-286

Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, Japan.

Dynamic functionality of mitochondria is maintained by continual fusion and fission events. A mitochondrial outer membrane protein Fzo1 plays a pivotal role upon mitochondrial fusion by homo-oligomerization to tether fusing mitochondria. Fzo1 is tightly regulated by ubiquitylations and the ubiquitin-responsible AAA protein Cdc48. Read More

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Dual roles of mitochondrial fusion gene FZO1 in yeast age asymmetry and in longevity mediated by a novel ATG32-dependent retrograde response.

Biogerontology 2019 02 8;20(1):93-107. Epub 2018 Oct 8.

Tulane Center for Aging and Department of Medicine, Tulane University Health Sciences Center, 1430 Tulane Ave., MBC 8513, New Orleans, LA, 70112, USA.

The replicative lifespan of the yeast Saccharomyces cerevisiae models the aging of stem cells. Age asymmetry between the mother and daughter cells is established during each cell division, such that the daughter retains the capacity for self-renewal while this ability is diminished in the mother. The segregation of fully-functional mitochondria to daughter cells is one mechanism that underlies this age asymmetry. Read More

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February 2019

Two Cdc48 cofactors Ubp3 and Ubx2 regulate mitochondrial morphology and protein turnover.

J Biochem 2018 Nov;164(5):349-358

Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Honjo 2-2-1, Chuo-ku, Kumamoto, Japan.

Mitochondria continuously undergo coordinated fusion and fission during vegetative growth to keep their homogeneity and to remove damaged components. A cytosolic AAA ATPase, Cdc48, is implicated in the mitochondrial fusion event and turnover of a fusion-responsible GTPase in the mitochondrial outer membrane, Fzo1, suggesting a possible linkage of mitochondrial fusion and Fzo1 turnover. Here, we identified two Cdc48 cofactor proteins, Ubp3 and Ubx2, involving mitochondria regulation. Read More

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November 2018

An ubiquitin-dependent balance between mitofusin turnover and fatty acids desaturation regulates mitochondrial fusion.

Nat Commun 2017 06 13;8:15832. Epub 2017 Jun 13.

Sorbonne Universités, UPMC University of Paris 06, CNRS, UMR8226, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, 75005 Paris, France.

Mitochondrial integrity relies on homotypic fusion between adjacent outer membranes, which is mediated by large GTPases called mitofusins. The regulation of this process remains nonetheless elusive. Here, we report a crosstalk between the ubiquitin protease Ubp2 and the ubiquitin ligases Mdm30 and Rsp5 that modulates mitochondrial fusion. Read More

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Ubiquitin-proteasome system and mitochondria - reciprocity.

Biochim Biophys Acta 2011 Feb 30;1809(2):80-7. Epub 2010 Jul 30.

Department of Biology, Technion - Israel Institute of Technology, Haifa, Israel.

Recently, sporadic links have been published between mitochondria - membrane-confined organelles - and the cytosolic ubiquitin-proteasome system (UPS) for removal of cellular proteins. For example, Fzo1, a mitochondrial outer membrane mitofusin was shown to be ubiquitinated by a ubiquitin ligase, Cdc53(MDM30), and degraded by the proteasome. Two additional ubiquitin ligases, MITOL/MARCH-V and MULAN, as well as a deubiquitinating enzyme, Ubp16/USP30, are embedded in mitochondrial outer membranes and participate in mitochondrial dynamics. Read More

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February 2011

A mutation associated with CMT2A neuropathy causes defects in Fzo1 GTP hydrolysis, ubiquitylation, and protein turnover.

Mol Biol Cell 2009 Dec 7;20(23):5026-35. Epub 2009 Oct 7.

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.

Charcot-Marie-Tooth disease type 2A (CMT2A) is caused by mutations in the gene MFN2 and is one of the most common inherited peripheral neuropathies. Mfn2 is one of two mammalian mitofusin GTPases that promote mitochondrial fusion and maintain organelle integrity. It is not known how mitofusin mutations cause axonal degeneration and CMT2A disease. Read More

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December 2009

The a2 mating-type-locus gene lga2 of Ustilago maydis interferes with mitochondrial dynamics and fusion, partially in dependence on a Dnm1-like fission component.

J Cell Sci 2009 Jul 16;122(Pt 14):2402-12. Epub 2009 Jun 16.

Max-Planck-Institute for Terrestrial Microbiology, Department Organismic Interactions, 35043 Marburg, Germany.

The a2 mating-type-locus gene lga2 of the basidiomycete Ustilago maydis encodes a mitochondrial protein that interferes with mitochondrial morphology and integrity, and that plays a role in uniparental inheritance of mitochondrial DNA. To address the mode of action of Lga2, we investigated its Dnm1 (a dynamin-related protein)-dependent effects. Here, we demonstrate that Dnm1 functions as a mitochondrial fission component in U. Read More

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Outer mitochondrial membrane protein degradation by the proteasome.

Novartis Found Symp 2007 ;287:4-14; discussion 14-20

Biochemistry Section, SNB, NINDS, NIH, Bethesda, MD 20892, USA.

Protein turnover is used for regulatory processes and to eliminate superfluous, denatured or chemically inactivated polypeptides. Mitochondrial proteins may be particularly susceptible to damage induced by reactive oxygen species and several pathways of mitochondrial proteolysis have been illuminated. However, in contrast to matrix and inner mitochondrial membrane protein degradation, little is known about the turnover of integral outer mitochondrial membrane (OMM) proteins or the mechanisms involved. Read More

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January 2008

Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1.

J Cell Biol 2006 Jun 30;173(5):645-50. Epub 2006 May 30.

Institute of Genetics and Center for Molecular Medicine, University of Cologne, D-50923 Cologne, Germany.

Mitochondrial morphology depends on balanced fusion and fission events. A central component of the mitochondrial fusion apparatus is the conserved GTPase Fzo1 in the outer membrane of mitochondria. Mdm30, an F-box protein required for mitochondrial fusion in vegetatively growing cells, affects the cellular Fzo1 concentration in an unknown manner. Read More

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