Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: Q9P021 and P78352 Pubmed SVM Score :0.0
NA
Interacting proteins: Q9P021 and P78352 Pubmed SVM Score :0.0
CRIPT , a novel postsynaptic protein that binds to the third PDZ domain of PSD 95 / SAP90 . ^^^ We report a novel protein , CRIPT , which is highly conserved from mammals to plants and binds selectively to the third PDZ domain ( PDZ 3 ) of PSD 95 via its C terminus . ^^^ In heterologous cells , CRIPT causes a redistribution of PSD 95 to microtubules . ^^^ In brain , CRIPT colocalizes with PSD 95 in the postsynaptic density and can be coimmunoprecipitated with PSD 95 and tubulin . ^^^ These findings suggest that CRIPT may regulate PSD 95 interaction with a tubulin based cytoskeleton in excitatory synapses . . ^^^
Interacting proteins: Q9P021 and P78352 Pubmed SVM Score :0.0
Microtubule binding by CRIPT and its potential role in the synaptic clustering of PSD 95 . ^^^ CRIPT is a postsynaptic protein that binds selectively to the third PDZ domain ( PDZ 3 ) of PSD 95 . ^^^ Here we show that CRIPT also binds directly to microtubules , thereby linking PSD 95 to the microtubule cytoskeleton . ^^^ Disrupting the CRIPT PSD 95 interaction in cultured hippocampal neurons with a PDZ 3 specific peptide prevented the association of PSD 95 with microtubules and inhibited the synaptic clustering of PSD 95 , chapsyn 110 / PSD 93 and GKAP ( a PSD 95 binding protein ) . ^^^
Interacting proteins: Q9P021 and P78352 Pubmed SVM Score :0.0
Here , using fluorescence anisotropy and NMR chemical shift analysis , we have characterized the association of PDZ 1 to the C terminal peptides of the GluR 6 subunit of the kainate receptor , voltage gated K ( + ) channel Kv1 . 4 , and microtubule associate protein CRIPT , all of which are known to associate with SAP 90 . ^^^
Interacting proteins: Q9P021 and P78352 Pubmed SVM Score :0.0
We also 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 . ^^^