In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-08-14)
Abstract:
To pass on information, the neurons that make up the nervous system connect at structures known as synapses. Chemical messengers called neurotransmitters are released from one neuron, and travel across the synapse to trigger a response in the neighbouring cell. The formation of new synapses plays an important role in learning and memory, but many aspects of this process are not well understood. In a specific region of the synapse called the active zone, a scaffold of proteins helps to release the neurotransmitters. These proteins are made in the cell body of the neuron, and are then transported to the end of the long, thin axons that protrude from the cell body. This presents a challenge for the cell, because the components of the active zone scaffold must be correctly targeted to the synapse at the end of the axon, ensuring the active zone scaffold assembles only at its proper location. Siebert, Böhme et al. studied how some of the proteins that are found in the active zone scaffold of the fruit fly Drosophila are transported along axons. Labelling the proteins with fluorescent markers allowed their movement to be examined under a microscope in living Drosophila larvae. The results showed that two of the proteins—known as BRP and RBP—are transported along the axons together. Further investigation revealed that a transport adaptor protein called Aplip1, which binds to RBP, is required for this movement. Siebert, Böhme et al. established the structure of the part of RBP where this interaction occurs, and found that mutating this region causes premature active zone scaffold assembly in the axonal part of the neuron. The interaction between RBP and Aplip1 is very strong, and this helps to prevent the scaffold assembling before it has reached the correct part of the neuron. Exactly how the transport adaptor and active zone protein are separated once they reach their final destination (the synapse) remains to be discovered.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.06935.001
DOI:
10.7554/eLife.06935.002
DOI:
10.7554/eLife.06935.003
DOI:
10.7554/eLife.06935.004
DOI:
10.7554/eLife.06935.005
DOI:
10.7554/eLife.06935.012
DOI:
10.7554/eLife.06935.013
DOI:
10.7554/eLife.06935.006
DOI:
10.7554/eLife.06935.007
DOI:
10.7554/eLife.06935.008
DOI:
10.7554/eLife.06935.009
DOI:
10.7554/eLife.06935.010
DOI:
10.7554/eLife.06935.011
DOI:
10.7554/eLife.06935.014
DOI:
10.7554/eLife.06935.015
DOI:
10.7554/eLife.06935.016
DOI:
10.7554/eLife.06935.017
DOI:
10.7554/eLife.06935.018
DOI:
10.7554/eLife.06935.019
DOI:
10.7554/eLife.06935.020
DOI:
10.7554/eLife.06935.021
DOI:
10.7554/eLife.06935.022
DOI:
10.7554/eLife.06935.023
DOI:
10.7554/eLife.06935.024
DOI:
10.7554/eLife.06935.025
DOI:
10.7554/eLife.06935.026
DOI:
10.7554/eLife.06935.027
DOI:
10.7554/eLife.06935.028
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3
