UMMS Affiliation

Program in Molecular Medicine; Brudnick Neuropsychiatric Research Institute; Department of Psychiatry

Date

9-15-2007

Document Type

Article

Disciplines

Biochemistry | Cell Biology | Cellular and Molecular Physiology | Developmental Biology | Molecular Biology

Abstract

JIP scaffold proteins are implicated in the regulation of protein kinase signal transduction pathways. To test the physiological role of these scaffold proteins, we examined the phenotype of compound mutant mice that lack expression of JIP proteins. These mice were found to exhibit severe defects in N-methyl-D-aspartic acid (NMDA) receptor function, including decreased NMDA-evoked current amplitude, cytoplasmic Ca(++), and gene expression. The decreased NMDA receptor activity in JIP-deficient neurons is associated with reduced tyrosine phosphorylation of NR2 subunits of the NMDA receptor. JIP complexes interact with the SH2 domain of cFyn and may therefore promote tyrosine phosphorylation and activity of the NMDA receptor. We conclude that JIP scaffold proteins are critically required for normal NMDA receptor function.

Rights and Permissions

Freely available online through the Genes and Development Open Access option. Citation: Genes Dev. 2007 Sep 15;21(18):2336-46. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Keywords

JIP, JNK, scaffold protein, signal transduction

PubMed ID

17875667

 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.