| First Author | Perez de Arce K | Year | 2010 |
| Journal | J Neurosci | Volume | 30 |
| Issue | 10 | Pages | 3728-38 |
| PubMed ID | 20220006 | Mgi Jnum | J:158978 |
| Mgi Id | MGI:4441007 | Doi | 10.1523/JNEUROSCI.2024-09.2010 |
| Citation | de Arce KP, et al. (2010) Synaptic clustering of PSD-95 is regulated by c-Abl through tyrosine phosphorylation. J Neurosci 30(10):3728-38 |
| abstractText | 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. |
