Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2013 May 14:2:e00804.
doi: 10.7554/eLife.00804.

Make or break for mitochondria

Catherine L Nezich  1 , Richard J Youle
Affiliations
Comment

Make or break for mitochondria

Catherine L Nezich et al. Elife. .

Abstract

Ensuring that mitochondrial DNA is successfully divided between daughter mitochondria involves a complex series of interactions with the endoplasmic reticulum and a variety of enzymes.

Keywords: ERMES; Gem1; Miro; S. cerevisiae; mitochondria; mitochondrial DNA.

PubMed Disclaimer

Conflict of interest statement

Competing interests:The authors declare that no competing interests exist.

Figures

Figure 1.
Figure 1.. Mitochondrial division.
(A) Murley et al. demonstrate that the ERMES tethering complex (pink) localizes to the region where the endoplasmic reticulum (ER) makes contact with a mitochondrion in yeast, and where the nucleoid that contains the mitochondrial DNA is replicating. (B) The mitochondrion undergoes constriction at this contact site, which allows a helix of Dnm1 (red) to form around it. (C) This helix leads to further constriction and, ultimately, to the division of the mitochondrion and the formation of two daughter mitochondria in wild-type cells (left). Each daughter mitochondrion has its own nucleoid. Significantly, one daughter remains attached to the ER via ERMES, which remains intact through the division process. However, in cells lacking Gem1, both of the daughter mitochondria remain tethered to the same ER segment, and both have somewhat unusual shapes (right).
See this image and copyright information in PMC

Comment on

References

    1. Boldogh IR, Nowakowski DW, Yang HC, Chung H, Karmon S, Royes P, et al. 2003. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol Biol Cell 14:4618–27 doi: 10.1091/mbc.E03-04-0225 - DOI - PMC - PubMed
    1. Friedman JR, Lackner LL, West M, DiBenedetto JR, Nunnari J, Voeltz GK. 2011. ER tubules mark sites of mitochondrial division. Science 334:358–62 doi: 10.1126/science.1207385 - DOI - PMC - PubMed
    1. Glater EE, Megeath LJ, Stowers RS, Schwarz TL. 2006. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J Cell Biol 173:545–57 doi: 10.1083/jcb.200601067 - DOI - PMC - PubMed
    1. Hobbs AEA, Srinivasan M, McCaffery JM, Jensen RE. 2001. Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability. J Cell Biol 152:401–10 doi: 10.1083/jcb.152.2.401 - DOI - PMC - PubMed
    1. Kornmann B, Currie E, Collins SR, Schuldiner M, Nunnari J, Weissman JS, et al. 2009. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325:477–81 doi: 10.1126/science.1175088 - DOI - PMC - PubMed

MeSH terms

LinkOut - more resources