Document Detail


Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae.
MedLine Citation:
PMID:  15760898     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mitochondria form a highly dynamic network that is shaped by continuous fission and fusion of these organelles. In the yeast Saccharomyces cerevisiae two machineries are involved in this process, one of which includes the mitochondrial fusion promoting GTPase Fzo1. Although a role for the F-box protein Mdm30 in regulating the stability of Fzo1 has been proposed, the molecular basis for the regulation of the fission to fusion ratio of mitochondria remains unknown. To discern the mechanism of the regulation of mitochondrial morphology, we arrested cells at different stages of the cell cycle and examined mitochondrial morphology as well as the stability of mitochondrial fission and fusion proteins. In response to a G1 arrest evoked by the mating pheromone alpha factor the mitochondrial network fragmented into small pieces, which was accompanied by dramatic down-regulation of Fzo1. Mating pheromone also triggered the degradation of Fzo1 produced under the control of a constitutive promoter, and Fzo1 was stabilized upon proteasome inhibition, indicating a role for the proteasome system in the degradation of Fzo1. However, deletion of MDM30 did not stabilize Fzo1 after mating pheromone treatment, showing a different mechanism from the previously reported process of steady state Fzo1 regulation. We show an example for a regulated change of the mitochondrial fission to fusion ratio during the life cycle of budding yeast. Proteasomal degradation of Fzo1 in response to the mating pheromone is proposed to mediate the remodeling of the mitochondrial network during the process of mating.
Authors:
Albert Neutzner; Richard J Youle
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Publication Detail:
Type:  Journal Article     Date:  2005-03-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  280     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2005 May 
Date Detail:
Created Date:  2005-05-09     Completed Date:  2005-07-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  18598-603     Citation Subset:  IM    
Affiliation:
Biochemistry Section, Surgical Neurological Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Cycle
DNA / metabolism
Down-Regulation
Drosophila
F-Box Proteins / chemistry
GTP Phosphohydrolases / chemistry*,  metabolism*
Gene Expression Regulation, Fungal*
Genes, Fungal
Green Fluorescent Proteins / chemistry
Membrane Proteins / chemistry*,  metabolism*
Microscopy, Confocal
Mitochondria / metabolism*
Mitochondrial Proteins / chemistry
Nocodazole / pharmacology
Pheromones / metabolism
Proteasome Endopeptidase Complex / chemistry,  metabolism
Saccharomyces cerevisiae / metabolism*
Saccharomyces cerevisiae Proteins / chemistry*,  metabolism*
Signal Transduction
Time Factors
Chemical
Reg. No./Substance:
0/F-Box Proteins; 0/Mdm30 protein, S cerevisiae; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/Pheromones; 0/Saccharomyces cerevisiae Proteins; 147336-22-9/Green Fluorescent Proteins; 31430-18-9/Nocodazole; 9007-49-2/DNA; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.6.1.-/FZO1 protein, S cerevisiae; EC 3.6.1.-/GTP Phosphohydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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