Identification and verification of novel rodent postsynaptic density proteins.
The postsynaptic density (PSD) is a cellular structure specialized in receiving and transducing synaptic information. Here we describe the identification of 452 proteins isolated from biochemically purified PSD fractions of rat and mouse brains using nanoflow HPLC coupled to electrospray tandem mass spectrometry (LC-MS/MS). Fluorescence microscopy and Western blotting were used to verify that many of the novel proteins identified exhibit subcellular distributions consistent with those of PSD-localized proteins. In addition to identifying most previously described PSD components, we also detected proteins involved in signaling to the nucleus as well as regulators of ADP-ribosylation factor signaling, ubiquitination, RNA trafficking, and protein translation. These results suggest new mechanisms by which the PSD helps regulate synaptic strength and transmission.
Jordan
Bryen A
BA
Department of Biochemistry, New York University, School of Medicine, NY 10016, USA.
Fernholz
Brian D
BD
Boussac
Muriel
M
Xu
Chongfeng
C
Grigorean
Gabriela
G
Ziff
Edward B
EB
Neubert
Thomas A
TA
D000818:Animals; D001923:Brain Chemistry; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D009474:Neurons / Q000737:chemistry; D040901:Proteomics; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013569:Synapses / Q000737:chemistry; D009435:Synaptic Transmission
D009419:Nerve Tissue Proteins; D011993:Recombinant Fusion Proteins