Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-12-21
pubmed:abstractText
Fyn, protein tyrosine kinase, and its substrates were highly concentrated in the postsynaptic density (PSD) fraction prepared from the rat forebrain. There were a number of Fyn substrates unique to the PSD fraction. One of the major substrates in the PSD fraction was found to be a concanavalin A-binding glycoprotein, PSD-gp180, which is the N-methyl-D-aspartate (NMDA) receptor subunit epsilon 2 (NR2B). Western blotting and immunoprecipitation supported the phosphorylation of epsilon 2 by Fyn. NMDA receptor subunit epsilon 1 (NR2A) was also a substrate for Fyn. These results suggest that Fyn is involved in the modulation of synaptic efficacy through the phosphorylation of synapse-specific substrates such as the NMDA receptor/channel.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
216
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
582-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
NMDA receptor subunits epsilon 1 (NR2A) and epsilon 2 (NR2B) are substrates for Fyn in the postsynaptic density fraction isolated from the rat brain.
pubmed:affiliation
Department of Biochemistry, Nagoya City University Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't