Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have characterized a high-affinity kainate binding site in in vitro living rat neocortical slices using [3H]kainate. [3H]Kainate labelled at least two binding sites, the higher affinity site with a Kd of 7.1 nM and a Bmax of 71.2 fmol/mg protein. This high-affinity binding site showed a pharmacology consistent with a kainate receptor with competition by kainate and domoic acid, as well as the (RS)-alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionate antagonist 6-cyano-2,3-dihydroxy-7-nitroquinoxaline. Increases in cellular depolarization induced by 2-h preincubations in veratridine and glutamate led to a significant 55% average decrease in [3H]kainate binding in adult cortex. Similarly, preincubation in kainate led to a significant average 26% decrease in binding. In both instances, Eadie-Hofstee analysis of saturation binding data revealed that the decreased binding reflected changes in receptor number. At different postnatal ages, increases in cellular depolarization significantly decreased binding (< 20 days postnatal age, -86%; > 60 days, -48%). Kainate treatment also significantly decreased binding at all ages (-64% at < 20 days; > 60 days, -18%), with significant differences noted between ages. These age-dependent effects are unlike those previously described for either N-methyl-D-aspartate [Lanius and Shaw (1992) Anat. Rec. 232, 54(A)] or (RS)-alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionate high affinity receptors [Shaw and Lanius (1992) Devl Brain Res. 68, 225-233].(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:High-affinity kainate binding sites in living slices of rat neocortex: characterization and regulation. 810 79

Protein palmitoylation is the most common posttranslational lipid modification; its reversibility mediates protein shuttling between intracellular compartments. A large family of DHHC (Asp-His-His-Cys) proteins has emerged as protein palmitoyl acyltransferases (PATs). However, mechanisms that regulate these PATs in a physiological context remain unknown. In this study, we efficiently monitored the dynamic palmitate cycling on synaptic scaffold PSD-95. We found that blocking synaptic activity rapidly induces PSD-95 palmitoylation and mediates synaptic clustering of PSD-95 and associated AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-type glutamate receptors. A dendritically localized DHHC2 but not the Golgi-resident DHHC3 mediates this activity-sensitive palmitoylation. Upon activity blockade, DHHC2 translocates to the postsynaptic density to transduce this effect. These data demonstrate that individual DHHC members are differentially regulated and that dynamic recruitment of protein palmitoylation machinery enables compartmentalized regulation of protein trafficking in response to extracellular signals.
 ...
PMID:Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95. 1959 46