In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-02-02)
Abstract:
Our brain contains billions of cells called neurons that form an extensive network through which information is readily exchanged. These cells connect to each other via junctions called synapses. Our developing brain starts off with far more synapses than it needs, but the excess synapses are destroyed as the brain matures. Even in adults, synapses are continuously made and destroyed in response to experiences and learning. Inside neurons there are tiny bubble-like compartments called vesicles that supply the synapses with many of the proteins and other components that they need. There is a growing body of evidence that suggests these vesicles are rapidly destroyed once a synapse is earmarked for destruction, but it is not clear how this may occur. Here, Binotti, Pavlos et al. found that a protein called Rab26 sits on the surface of the vesicles near synapses. This protein promotes the formation of clusters of vesicles, and a membrane sometimes surrounds these clusters. Further experiments indicate that several proteins involved in a process called autophagy—where unwanted proteins and debris are destroyed—may also be found around the clusters of vesicles. Autophagy starts with the formation of a membrane around the material that needs to be destroyed. This seals the material off from rest of the cell so that enzymes can safely break it down. Binotti, Pavlos et al. found that one of the autophagy proteins—called Atg16L—can bind directly to Rab26, but only when Rab26 is in an ‘active’ state. These findings suggest that excess vesicles at synapses may be destroyed by autophagy. Further work will be required to establish how this process is controlled and how it is involved in the loss of synapses.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.05597.001
DOI:
10.7554/eLife.05597.002
DOI:
10.7554/eLife.05597.003
DOI:
10.7554/eLife.05597.004
DOI:
10.7554/eLife.05597.005
DOI:
10.7554/eLife.05597.006
DOI:
10.7554/eLife.05597.007
DOI:
10.7554/eLife.05597.008
DOI:
10.7554/eLife.05597.009
DOI:
10.7554/eLife.05597.010
DOI:
10.7554/eLife.05597.011
DOI:
10.7554/eLife.05597.012
DOI:
10.7554/eLife.05597.013
DOI:
10.7554/eLife.05597.014
DOI:
10.7554/eLife.05597.015
DOI:
10.7554/eLife.05597.016
DOI:
10.7554/eLife.05597.017
DOI:
10.7554/eLife.05597.018
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3
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