In:
eLife, eLife Sciences Publications, Ltd, Vol. 6 ( 2017-05-17)
Abstract:
Animal cells produce many small proteins known as peptides that help cells to communicate with each other. To become active, many of these peptides need to be chemically modified. PAM is the only enzyme that carries out a type of peptide modification called amidation and it is essential for animals to grow and survive. PAM was originally thought to have evolved in the nervous system of animals, but recent studies have found that it is also present in green algae and in hair-like projections known as cilia, which are found on the surface of most animal cells. There are two types of cilia: motile cilia beat rhythmically and are responsible for moving cells and fluids, while non-motile cilia sense the external environment and serve as signaling hubs. These observations suggest that PAM may have other roles in cells in addition to activating peptides. Kumar et al. now set out to investigate the role of PAM in green algae, flatworms and mice. The results show that PAM is important for the formation of both motile and non-motile cilia. Reducing the levels of PAM in the algae and flatworms resulted in short stubs forming on the surface of cells instead of motile cilia. This reduced the ability of flatworms to glide around their environment. Furthermore, the cells of mutant mice lacking PAM produced non-motile cilia that were much shorter than those produced by normal mouse cells. Further experiments suggest that PAM may be involved in the transport of certain proteins to the sites where new cilia will form. The findings of Kumar et al. reveal a link between the PAM enzyme, amidation and the assembly of cilia. The next step will be to identify the molecules that are modified by PAM and work out exactly how amidated products might regulate the formation of cilia.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.25728.001
DOI:
10.7554/eLife.25728.002
DOI:
10.7554/eLife.25728.003
DOI:
10.7554/eLife.25728.004
DOI:
10.7554/eLife.25728.005
DOI:
10.7554/eLife.25728.006
DOI:
10.7554/eLife.25728.007
DOI:
10.7554/eLife.25728.008
DOI:
10.7554/eLife.25728.009
DOI:
10.7554/eLife.25728.010
DOI:
10.7554/eLife.25728.011
DOI:
10.7554/eLife.25728.012
DOI:
10.7554/eLife.25728.013
DOI:
10.7554/eLife.25728.014
DOI:
10.7554/eLife.25728.015
DOI:
10.7554/eLife.25728.016
DOI:
10.7554/eLife.25728.017
DOI:
10.7554/eLife.25728.018
DOI:
10.7554/eLife.25728.019
DOI:
10.7554/eLife.25728.020
DOI:
10.7554/eLife.25728.021
DOI:
10.7554/eLife.25728.022
DOI:
10.7554/eLife.25728.023
DOI:
10.7554/eLife.25728.024
DOI:
10.7554/eLife.25728.025
DOI:
10.7554/eLife.25728.026
DOI:
10.7554/eLife.25728.027
DOI:
10.7554/eLife.25728.028
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2017
detail.hit.zdb_id:
2687154-3