In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-04-14)
Abstract:
In all animals, it is important that cells are correctly organised into tissues and organs. This organisation starts in the embryo, and cells are instructed to perform different roles depending on their position within the body. A family of proteins called the Hox proteins coordinates the organisation of the cells in the animal embryo by binding to and controlling the expression of specific genes. To properly control their target genes, Hox proteins need to interact with other proteins called transcription factors that can also bind to the genes. However, only a few of these transcription factors have been identified so far, and it is not clear how Hox proteins are able to interact with them. Here, Baëza, Viala, Heim et al. identified several more transcription factors that can bind to the Hox proteins in fruit fly embryos. The experiments show that Hox proteins are able to bind to many transcription factors that are very different from each other. Baëza, Viala, Heim et al. also show that two short sections within the Hox proteins known as short linear motifs are important for controlling these interactions. A fly Hox protein that was missing these motifs was able to interact with new transcription factors. This inhibitory role was found in Hox proteins from mice and sea anemones, suggesting that these motifs may play the same role in all animals. Baëza, Viala, Heim et al.'s findings challenge the traditional view of the role of the short linear motifs in interactions between proteins. Also, the findings provide an alternative explanation for how the Hox proteins are only able to interact with particular transcription factors in animal embryos. The next step will be to find out whether the inhibitory role of short linear motifs could more generally apply to many other protein families.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.06034.001
DOI:
10.7554/eLife.06034.002
DOI:
10.7554/eLife.06034.003
DOI:
10.7554/eLife.06034.004
DOI:
10.7554/eLife.06034.005
DOI:
10.7554/eLife.06034.006
DOI:
10.7554/eLife.06034.007
DOI:
10.7554/eLife.06034.008
DOI:
10.7554/eLife.06034.009
DOI:
10.7554/eLife.06034.010
DOI:
10.7554/eLife.06034.011
DOI:
10.7554/eLife.06034.012
DOI:
10.7554/eLife.06034.013
DOI:
10.7554/eLife.06034.014
DOI:
10.7554/eLife.06034.015
DOI:
10.7554/eLife.06034.016
DOI:
10.7554/eLife.06034.017
DOI:
10.7554/eLife.06034.018
DOI:
10.7554/eLife.06034.019
DOI:
10.7554/eLife.06034.020
DOI:
10.7554/eLife.06034.021
DOI:
10.7554/eLife.06034.022
DOI:
10.7554/eLife.06034.023
DOI:
10.7554/eLife.06034.024
DOI:
10.7554/eLife.06034.025
DOI:
10.7554/eLife.06034.026
DOI:
10.7554/eLife.06034.027
DOI:
10.7554/eLife.06034.028
DOI:
10.7554/eLife.06034.029
DOI:
10.7554/eLife.06034.030
DOI:
10.7554/eLife.06034.031
DOI:
10.7554/eLife.06034.032
DOI:
10.7554/eLife.06034.033
DOI:
10.7554/eLife.06034.034
DOI:
10.7554/eLife.06034.035
DOI:
10.7554/eLife.06034.036
DOI:
10.7554/eLife.06034.037
DOI:
10.7554/eLife.06034.038
DOI:
10.7554/eLife.06034.039
DOI:
10.7554/eLife.06034.040
DOI:
10.7554/eLife.06034.041
DOI:
10.7554/eLife.06034.042
DOI:
10.7554/eLife.06034.043
DOI:
10.7554/eLife.06034.044
DOI:
10.7554/eLife.06034.045
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3
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