CRIPT, a Novel Postsynaptic Protein that Binds to the Third PDZ Domain of PSD-95/SAP90

@article{Niethammer1998CRIPTAN,
  title={CRIPT, a Novel Postsynaptic Protein that Binds to the Third PDZ Domain of PSD-95/SAP90},
  author={Martin Niethammer and Juli G. Valtschanoff and Tarun M. Kapoor and Daniel W. Allison and Richard J. Weinberg and Ann Marie Craig and Morgan Sheng},
  journal={Neuron},
  year={1998},
  volume={20},
  pages={693-707}
}

Figures from this paper

Interaction Between CRIPT and PSD-95 Is Required for Proper Dendritic Arborization in Hippocampal Neurons
TLDR
It is shown that overexpression of a full-length CRIPT leads to a modest decrease, and knockdown of CRIPt leads to an increase in dendritic branching in cultured rat hippocampal neurons, and the significance of the interaction betweenCRIPT and the third PDZ domain of PSD-95 is underscored.
Selectivity and Promiscuity of the First and Second PDZ Domains of PSD-95 and Synapse-associated Protein 102*
TLDR
The studies indicate that all of the last five residues of NR2b contribute to the binding selectivity of the prototypic interactions of the PDZ domains of postsynaptic density protein 95 and its homolog synapse-associated protein 90 (SAP102) with theNR2b subunit of theN-methyl-d-aspartate-type glutamate receptor.
Requirement of N-terminal Cysteines of PSD-95 for PSD-95 Multimerization and Ternary Complex Formation, but Not for Binding to Potassium Channel Kv1.4*
TLDR
It is suggested that the N-terminal cysteine residues are essential for PSD-95 multimerization and thatMultimerization is required for simultaneous binding of multiple membrane protein ligands by PSd-95.
Ligand Binding of the Second PDZ Domain Regulates Clustering of PSD-95 with the Kv1.4 Potassium Channel*
TLDR
This study suggests that the correct placement of the multiple domains in the full-length PSD-95 protein is necessary for the optimal protein activity, and shows that PDZ2, which is endowed with the highest affinity for Kv1.4, is required for efficient ligand binding.
Essential Contribution of the Ligand-Binding βB/βC Loop of PDZ1 and PDZ2 in the Regulation of Postsynaptic Clustering, Scaffolding, and Localization of Postsynaptic Density-95
TLDR
The ligand-binding affinity of the PDZ domains of PSD-95, contributed in part via its interaction with the C-terminal end of synGAP, plays a critical role in titrating the synaptic clustering of PSd-95 and controlling its tight association with the PSD scaffold, thereby affecting synapse maturation.
The interaction between PSD-95 and Ca2+/calmodulin is enhanced by PDZ-binding proteins.
TLDR
It is found that C-terminal peptides from proteins such as CRIPT and the N-methyl-d-aspartate receptor NR2B subunit, which associate with the PDZ domain of PSD-95, enhanced the affinity of PSd-95 for calmodulin.
Microtubule binding by CRIPT and its potential role in the synaptic clustering of PSD-95
TLDR
It is shown that CRIPT also binds directly to microtubules, thereby linking PSD-95 to the microtubule cytoskeleton, suggesting that PSD -95-family proteins are not essential for the maintenance of synapses and the synaptic localization of NMDA receptors.
Ligand binding to the PDZ domains of postsynaptic density protein 95.
TLDR
A systematic study on the ligand-binding kinetics of Postsynaptic density protein 95 using constructs of different size for PSD-95 and its ligands and found that residues outside of the canonical binding pocket modulate the affinity of the ligands.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 143 REFERENCES
Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
  • M. Niethammer, E. Kim, M. Sheng
  • Biology, Chemistry
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1996
TLDR
Data suggest that PDZ domains can function as modules for protein-protein interactions and members of the PSD-95 family might serve to anchor NMDA receptors to the submembrane cytoskeleton and aid in the assembly of signal transduction complexes at postsynaptic sites.
GKAP, a Novel Synaptic Protein That Interacts with the Guanylate Kinase-like Domain of the PSD-95/SAP90 Family of Channel Clustering Molecules
TLDR
The isolation of a novel synaptic protein, termed GKAP for guanylate kinase-associated protein, that binds directly to the GK domain of the four known members of the mammalian PSD-95 family, shows a unique domain structure and appears to be a major constituent of the postsynaptic density.
Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton
TLDR
A mechanism by which PDZ domain-binding proteins may be coupled to ATP and the membrane cytoskeleton via hDlg is suggested through a combination of protease digestion and in vitro binding measurements.
Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
TLDR
Light and immunoelectron microscopic analysis of the rat hippocampal formation revealed that SAP97 is localized in the presynaptic nerve termini of excitatory synapses, suggesting that members of the SAP90/SAP97 subfamily may be involved in the site specific assembly, stability or functions of membrane specialization at sites of cell-cell contact.
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
TLDR
The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses.
SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A.
...
1
2
3
4
5
...