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Synaptic clustering of PSD-95 is regulated by c-Abl through tyrosine phosphorylation.

Authors: Perez de Arce, K  Varela-Nallar, L  Farias, O  Cifuentes, A  Bull, P  Couch, BA  Koleske, AJ  Inestrosa, NC  Alvarez, AR 
Citation: Perez de Arce K, etal., J Neurosci. 2010 Mar 10;30(10):3728-38. doi: 10.1523/JNEUROSCI.2024-09.2010.
Pubmed: (View Article at PubMed) PMID:20220006
DOI: Full-text: DOI:10.1523/JNEUROSCI.2024-09.2010

The c-Abl tyrosine kinase is present in mouse brain synapses, but its precise synaptic function is unknown. We found that c-Abl levels in the rat hippocampus increase postnatally, with expression peaking at the first postnatal week. In 14 d in vitro hippocampal neuron cultures, c-Abl localizes primarily to the postsynaptic compartment, in which it colocalizes with the postsynaptic scaffold protein postsynaptic density protein-95 (PSD-95) in apposition to presynaptic markers. c-Abl associates with PSD-95, and chemical or genetic inhibition of c-Abl kinase activity reduces PSD-95 tyrosine phosphorylation, leading to reduced PSD-95 clustering and reduced synapses in treated neurons. c-Abl can phosphorylate PSD-95 on tyrosine 533, and mutation of this residue reduces the ability of PSD-95 to cluster at postsynaptic sites. Our results indicate that c-Abl regulates synapse formation by mediating tyrosine phosphorylation and clustering of PSD-95.


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RGD ID: 8693579
Created: 2014-07-16
Species: All species
Last Modified: 2014-07-16
Status: ACTIVE


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