Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 187, Issue 2, Pages 187-193Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2014.05.010
Keywords
Cdc48p/p97; AAA ATPase; Mitochondrial morphology; Mitochondrial fusion; Protein degradation; Serial block-face SEM
Funding
- JSPS
- MEXT, Japan
- Joint Usage/Research Center for Developmental Medicine
- Institute of Molecular Embryology and Genetics, Kumamoto University, Japan
- NIPS, Japan
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Cdc48p is a highly conserved cytosolic AAA chaperone that is involved in a wide range of cellular processes. It consists of two ATPase domains (D1 and D2), with regulatory regions at the N- and C-terminals. We have recently shown that Cdc48p regulates mitochondrial morphology, in that a loss of the ATPase activity or positive cooperativity in the D2 domain leads to severe fragmentations and aggregations of mitochondria in the cytoplasm. We have now used serial block-face scanning electron microscopy (SBF-SEM), an advanced three-dimensional (3D) electron microscopic technique to examine the structures and morphological changes of mitochondria in the yeast Saccharomyces cerevisiae. We found that mutants lacking ATPase activity of Cdc48p showed mitochondrial fragmentations and aggregations, without fusion of the outer membrane. This suggests that the ATPase activity of Cdc48p is necessary for fusion of the outer membranes of mitochondria. Our results also show that SBF-SEM has considerable advantages in morphological and quantitative studies on organelles and intracellular structures in entire cells. (C) 2014 Elsevier Inc. All rights reserved.
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