PDZ domain proteins of synapses
Top Cited Papers
- 1 October 2004
- journal article
- review article
- Published by Springer Nature in Nature Reviews Neuroscience
- Vol. 5 (10) , 771-781
- https://doi.org/10.1038/nrn1517
Abstract
PDZ domains are protein-interaction domains that are often found in multi-domain scaffolding proteins. PDZ-containing scaffolds assemble specific proteins into large molecular complexes at defined locations in the cell. In the postsynaptic density of neuronal excitatory synapses, PDZ proteins such as PSD-95 organize glutamate receptors and their associated signalling proteins and determine the size and strength of synapses. PDZ scaffolds also function in the dynamic trafficking of synaptic proteins by assembling cargo complexes for transport by molecular motors. As key organizers that control synaptic protein composition and structure, PDZ scaffolds are themselves highly regulated by synthesis and degradation, subcellular distribution and post-translational modification.Keywords
This publication has 147 references indexed in Scilit:
- The Serotonin 5-HT2A and 5-HT2C Receptors Interact with Specific Sets of PDZ ProteinsJournal of Biological Chemistry, 2004
- Calcium/Calmodulin-dependent Protein Kinase II Phosphorylation Drives Synapse-associated Protein 97 into SpinesPublished by Elsevier ,2004
- Regulation of the Neuron-specific Ras GTPase-activating Protein, synGAP, by Ca2+/Calmodulin-dependent Protein Kinase IIJournal of Biological Chemistry, 2004
- Tamalin Is a Scaffold Protein That Interacts with Multiple Neuronal Proteins in Distinct Modes of Protein-Protein AssociationJournal of Biological Chemistry, 2003
- Interaction of the Tyrosine Kinase Pyk2 with the N-Methyl-d-aspartate Receptor Complex via the Src Homology 3 Domains of PSD-95 and SAP102Published by Elsevier ,2003
- Direct Interaction with a Kinesin-related Motor Mediates Transport of Mammalian Discs Large Tumor Suppressor Homologue in Epithelial CellsJournal of Biological Chemistry, 2003
- Crystal Structure of GRIP1 PDZ6-Peptide Complex Reveals the Structural Basis for Class II PDZ Target Recognition and PDZ Domain-mediated MultimerizationPublished by Elsevier ,2003
- G Protein-coupled Receptor Kinase 5 Regulates β1-Adrenergic Receptor Association with PSD-95Published by Elsevier ,2002
- The ERBB2/HER2 Receptor Differentially Interacts with ERBIN and PICK1 PSD-95/DLG/ZO-1 Domain ProteinsJournal of Biological Chemistry, 2001
- Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinasesNature, 1995