Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Display Documents



  history
ID: 270923.0, MPI für biophysikalische Chemie / Abteilungsunabhängige Arbeitsgruppen
A unique PDZ ligand in PKCalpha confers induction of cerebellar long-term synaptic depression.
Authors:Leitges, M.; Kovac, J.; Plomann, M.; Linden, D. J.
Language:English
Date of Publication (YYYY-MM-DD):2004-11-18
Title of Journal:Neuron
Volume:44
Issue / Number:4
Start Page:585
End Page:594
Review Status:not specified
Audience:Not Specified
Abstract / Description:Induction of cerebellar long-term depression (LTD) requires a postsynaptic cascade involving activation of mGluR1 and protein kinase C (PKC). Our understanding of this process has been limited by the fact that PKC is a large family of molecules, many isoforms of which are expressed in the relevant postsynaptic compartment, the cerebellar Purkinje cell. Here, we report that LTD is absent in Purkinje cells in which the alpha isoform of PKC has been reduced by targeted RNA interference or in cells derived from PKCalpha null mice. In both of these cases, LTD could be rescued by expression of PKCalpha but not other PKC isoforms. The special role of PKCalpha in cerebellar LTD is likely to derive from its unique PDZ ligand (QSAV). When this motif is mutated, PKCalpha no longer supports LTD. Conversely, when this PDZ ligand is inserted in a nonpermissive isoform, PKCgamma, it confers the capacity for LTD induction.
Free Keywords:3T3 Cells; Animals; Humans; Isoenzymes/genetics/metabolism; Ligands; Long-Term Depression (Physiology)/physiology; Mice; Patch-Clamp Techniques; Protein Kinase C/genetics/metabolism
Protein-Serine-Threonine Kinases/metabolism; Purkinje Cells/enzymology; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Synapses/physiology; Transfection
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/AG Leitges
MPI für biophysikalische Chemie/Abt. Eichele
Identifiers:URL:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=...
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.