mSYD1A, a Mammalian Synapse-Defective-1 Protein, Regulates Synaptogenic Signaling and Vesicle Docking
Neuron. 2013-06-01; 78(6): 1012-1023
DOI: 10.1016/j.neuron.2013.05.010
Read on PubMed
1. Neuron. 2013 Jun 19;78(6):1012-23. doi: 10.1016/j.neuron.2013.05.010.
mSYD1A, a mammalian synapse-defective-1 protein, regulates synaptogenic signaling
and vesicle docking.
Wentzel C(1), Sommer JE, Nair R, Stiefvater A, Sibarita JB, Scheiffele P.
Author information:
(1)Biozentrum, University of Basel, 4056 Basel, Switzerland.
Structure and function of presynaptic terminals are critical for the transmission
and processing of neuronal signals. Trans-synaptic signaling systems instruct the
differentiation and function of presynaptic release sites, but their downstream
mediators are only beginning to be understood. Here, we identify the
intracellular mSYD1A (mouse Synapse-Defective-1A) as a regulator of presynaptic
function in mice. mSYD1A forms a complex with presynaptic receptor tyrosine
phosphatases and controls tethering of synaptic vesicles at synapses. mSYD1A
function relies on an intrinsically disordered domain that interacts with
multiple structurally unrelated binding partners, including the active zone
protein liprin-α2 and nsec1/munc18-1. In mSYD1A knockout mice, synapses assemble
in normal numbers but there is a significant reduction in synaptic vesicle
docking at the active zone and an impairment of synaptic transmission. Thus,
mSYD1A is a regulator of presynaptic release sites at central synapses.
Copyright © 2013 Elsevier Inc. All rights reserved.
DOI: 10.1016/j.neuron.2013.05.010
PMCID: PMC3719036
PMID: 23791195 [Indexed for MEDLINE]