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

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.

Pubmed ID: 20220006 RIS Download

Mesh terms: Animals | Biomarkers | Cell Line | Cells, Cultured | Humans | Intracellular Signaling Peptides and Proteins | Male | Membrane Proteins | Mice | Mice, Knockout | Phosphorylation | Proto-Oncogene Proteins c-abl | Rats | Rats, Sprague-Dawley | Synapses | Tyrosine

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Associated grants

  • Agency: NINDS NIH HHS, Id: R01 NS039475
  • Agency: NINDS NIH HHS, Id: R01 NS039475-08
  • Agency: NINDS NIH HHS, Id: NS39475

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