In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-04-21)
Abstract:
Our actions often depend on who we interact with: parents, teachers, friends, colleagues. So it is for proteins in the cell: their function depends on which other proteins they work with. If a protein interacts with new partners or ends up in a new neighborhood of the cell, it can perform an entirely unexpected role, rewiring how that cell works. There are millions of possible protein-protein interactions, but it is not known how cells behave if their proteins are forced into new associations. For example, how many of these associations affect how well the cell can grow? Using budding yeast, Berry et al. were able to associate every protein in the cell with proteins from each of the major areas of the cell such as the nucleus, cell membrane or mitochondria. These new associations and relocations were then examined to see how many of them caused problems, slowing the cell’s growth or killing it. Unexpectedly, most forced associations had no detectable effect, indicating that the cell is remarkably tolerant of new protein-protein interactions. This contradicts a common idea that proteins are very fussy about their partner proteins, and will not work properly if they are forced into new interactions. The associations that do cause a growth defect are often between proteins that normally work together, indicating that their association is normally carefully controlled during the normal growth of cells. In some cases these forced associations identified previously unknown regulators of cell behavior. Proteins that interact with the wrong partners or are in the wrong place within cells cause a number of diseases. Future forced association experiments will allow us to examine such interactions and possibly search for drugs that will correct the problem.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.13053.001
DOI:
10.7554/eLife.13053.002
DOI:
10.7554/eLife.13053.003
DOI:
10.7554/eLife.13053.004
DOI:
10.7554/eLife.13053.005
DOI:
10.7554/eLife.13053.006
DOI:
10.7554/eLife.13053.007
DOI:
10.7554/eLife.13053.008
DOI:
10.7554/eLife.13053.009
DOI:
10.7554/eLife.13053.010
DOI:
10.7554/eLife.13053.011
DOI:
10.7554/eLife.13053.012
DOI:
10.7554/eLife.13053.013
DOI:
10.7554/eLife.13053.014
DOI:
10.7554/eLife.13053.015
DOI:
10.7554/eLife.13053.016
DOI:
10.7554/eLife.13053.017
DOI:
10.7554/eLife.13053.018
DOI:
10.7554/eLife.13053.019
DOI:
10.7554/eLife.13053.020
DOI:
10.7554/eLife.13053.021
DOI:
10.7554/eLife.13053.022
DOI:
10.7554/eLife.13053.023
DOI:
10.7554/eLife.13053.024
DOI:
10.7554/eLife.13053.025
DOI:
10.7554/eLife.13053.030
DOI:
10.7554/eLife.13053.031
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2016
detail.hit.zdb_id:
2687154-3