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Actin‐binding proteins in a postsynaptic preparation: Lasp‐1 is a component of central nervous system synapses and dendritic spines
Author(s) -
Phillips Greg R.,
Anderson Tonya R.,
Florens Laurence,
Gudas Christopher,
Magda Gabriela,
Yates John R.,
Colman David R.
Publication year - 2004
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20224
Subject(s) - postsynaptic potential , postsynaptic density , actin remodeling of neurons , dendritic spine , synaptic plasticity , actin binding protein , microbiology and biotechnology , neuroscience , neurotransmission , actin , synapse , biology , actin remodeling , chemistry , inhibitory postsynaptic potential , actin cytoskeleton , cytoskeleton , excitatory postsynaptic potential , biochemistry , cell , receptor , hippocampal formation
CNS synapses are complex sites of cell–cell communication. Identification and characterization of the protein components of synapses will lead to a better understanding of the mechanisms of neurotransmission and plasticity. We applied multidimensional protein identification technology (MudPIT) to purified, guanidine‐solubilized postsynaptic fractions to identify novel synaptically localized molecules. We identified several actin‐associated proteins known to regulate actin polymerization and control cell motility in nonneural cells that have not previously been associated with CNS synaptic function. One of these is lasp‐1, an actin‐associated LIM and SH3 domain‐containing protein. We show that lasp‐1 is strongly expressed by CNS neurons and is concentrated at synaptic sites. Overall, the preponderance of actin‐associated proteins in postsynaptic density fractions, and specifically those involved in actin reorganization, suggests that there are many modes by which the state of synaptic F‐actin polymerization and, hence, synaptic physiology are affected. © 2004 Wiley‐Liss, Inc.