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Cooperation of Syd-1 with Neurexin synchronizes pre- with postsynaptic assembly
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Cooperation of Syd-1 with Neurexin synchronizes pre- with postsynaptic assembly
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Cooperation of Syd-1 with Neurexin synchronizes pre- with postsynaptic assembly
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Journal Article
Cooperation of Syd-1 with Neurexin synchronizes pre- with postsynaptic assembly
2012
Overview
The
Drosophila
proteins Neuroligin (Nlg1) and Neurexin (Nrx-1) form a trans-synaptic complex that regulates synapse formation at the neuromuscular junction. Here the authors show that Syd-1, also known to regulate active zone formation, interacts with presynaptic Nrx-1, promoting synaptic clustering and immobilization of Nrx-1, and subsequent glutamate receptor incorporation.
Synapse formation and maturation requires bidirectional communication across the synaptic cleft. The trans-synaptic Neurexin-Neuroligin complex can bridge this cleft, and severe synapse assembly deficits are found in
Drosophila melanogaster neuroligin (Nlg1
,
dnlg1)
and
neurexin
(
Nrx-1
,
dnrx
) mutants. We show that the presynaptic active zone protein Syd-1 interacts with Nrx-1 to control synapse formation at the
Drosophila
neuromuscular junction. Mutants in
Syd-1
(
RhoGAP100F
,
dsyd-1
),
Nrx-1
and
Nlg1
shared active zone cytomatrix defects, which were nonadditive. Syd-1 and Nrx-1 formed a complex
in vivo
, and Syd-1 was important for synaptic clustering and immobilization of Nrx-1. Consequently, postsynaptic clustering of Nlg1 was affected in
Syd-1
mutants, and
in vivo
glutamate receptor incorporation was changed in
Syd-1
,
Nrx-1
and
Nlg1
mutants.
S
tabilization of nascent Syd-1–Liprin-α (DLiprin-α) clusters, important to initialize active zone formation, was Nlg1 dependent. Thus, cooperation between Syd-1 and Nrx-1–Nlg1 seems to orchestrate early assembly processes between pre- and postsynaptic membranes, promoting avidity of newly forming synaptic scaffolds.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Animal Genetics and Genomics
/ Animals
/ Biomedical and Life Sciences
/ Cell Adhesion Molecules - physiology
/ Cell Adhesion Molecules, Neuronal - genetics
/ Cell Adhesion Molecules, Neuronal - physiology
/ Drosophila Proteins - genetics
/ Drosophila Proteins - metabolism
/ Drosophila Proteins - physiology
/ GTPase-Activating Proteins - genetics
/ GTPase-Activating Proteins - physiology
/ Insects
/ Neuromuscular Junction - physiology
/ Phosphoproteins - metabolism
/ Presynaptic Terminals - physiology
/ Proteins
/ Receptors, Glutamate - physiology
/ Saccharomyces cerevisiae - genetics
/ Synapses
