English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family

Köhr, G., & Seeburg, P. H. (1996). Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family. Physiology, 492(2), 445-452. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/9019541/.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family

Files

show Files
hide Files
:
JPhysiol_492_1996_445.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
JPhysiol_492_1996_445.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Köhr, Georg1, Author              
Seeburg, Peter H.1, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

Content

show
hide
Free keywords: -
 Abstract: 1. Tyrosine kinases regulate NMDA receptor-channel activity in cultured neurons, and NMDA receptor subunits are tyrosine phosphorylated in the brain. 2. Heteromeric NMDA receptor-channels were transiently expressed in human embryonic kidney (HEK) 293 cells and glutamate (100 microM)-activated whole-cell currents (500 ms) were studied when tyrosine kinases of the src gene family were included in the pipette solution. 3. Glutamate-activated currents (evoked every 20 s for up to 20 min) were increased by src and fyn kinases without affecting the desensitization and deactivation kinetics in NR1-NR2A but the kinases had no effects in NR1-NR2B, NR1-NR2C and NR1-NR2D receptor-channels, suggesting that a phosphorylation site in NR2A is targeted. 4. In a mutant channel consisting of NR1 and a C-terminal deletion mutant of NR2A (NR2A delta C), src and fyn kinases lost their potentiating effects indicating that the phosphorylation of tyrosine(s) in the C-terminal domain of NR2A affects the current flux through native NMDA receptor-channels.

Details

show
hide
Language(s): eng - English
 Dates: 1996-01-021996-02-221996-04-15
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Physiology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Bethesda, Md. : International Union of Physiological Sciences :
Pages: - Volume / Issue: 492 (2) Sequence Number: - Start / End Page: 445 - 452 Identifier: ISSN: 1548-9213
CoNE: https://pure.mpg.de/cone/journals/resource/954925552377