In:
eLife, eLife Sciences Publications, Ltd, Vol. 3 ( 2014-04-08)
Abstract:
Respiration is vital to all living things because it is the process by which nutrients are converted into useful energy. Within our cells, organelles called mitochondria harness this energy and store it within molecules of ATP. This energy can then be released, when it is needed, by breaking down an ATP molecule into simpler chemicals. When viewed under an electron microscope, it can be seen that an individual mitochondrion has two membranes: a highly folded inner membrane, and an outer membrane that is fairly smooth. However, some of the genes, proteins and other molecules that determine the complex shapes of mitochondria have not been identified. Using a technique called mass spectrometry, a protein called Aim24 was previously shown to accumulate at the sites where the two membranes of a mitochondrion make contact with each other. Now, Harner et al. have discovered that Aim24 proteins are transported into mitochondria and embedded within the inner membranes. Aim24 is needed to assemble and maintain the stability of the protein complex that anchors the inner membrane to the outer membrane: mitochondria that lack the Aim24 protein have an irregular structure. Furthermore, Harner et al. showed that Aim24 is needed to form other protein complexes—also within the inner membrane—that work together to harness the energy that is released when nutrients are broken down, so that it can be stored as ATP. Cells that lack the Aim24 gene also showed changes in the kinds of molecules found within the membranes of the mitochondria. This work shows how difficult it can be to determine how the shapes of structures within cells, such as mitochondria, are controlled—as one protein can have many roles that cannot be easily teased apart. The on-going challenge is to uncover how different proteins, and other molecules in the membranes of mitochondria, interact to determine the structure, and consequently function, of the mitochondria in a cell.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.01684.001
DOI:
10.7554/eLife.01684.002
DOI:
10.7554/eLife.01684.003
DOI:
10.7554/eLife.01684.004
DOI:
10.7554/eLife.01684.005
DOI:
10.7554/eLife.01684.006
DOI:
10.7554/eLife.01684.007
DOI:
10.7554/eLife.01684.008
DOI:
10.7554/eLife.01684.009
DOI:
10.7554/eLife.01684.010
DOI:
10.7554/eLife.01684.011
DOI:
10.7554/eLife.01684.012
DOI:
10.7554/eLife.01684.013
DOI:
10.7554/eLife.01684.014
DOI:
10.7554/eLife.01684.015
DOI:
10.7554/eLife.01684.016
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2014
detail.hit.zdb_id:
2687154-3
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