| Interaction ID | Mol A | Type | Species | Verb | Nature | Mol B | Type | Species |   |
|---|
|
| 74265 | CDK5R1 | Protein | Homo sapiens-e | Increases activity | direct | CDK5 | Protein | Homo sapiens | | | Cdk5 is activated by the association with its
regulatory partner p35 or its truncated form, p25, which is
elevated in AD brains. /In this study, we investigated
APP(Thr668) phosphorylation and APP processing mediated by
p35/Cdk5 and p25/Cdk5 in the human neuroblastoma cell line
SH-SY5Y. / These results confirm the involvement of Cdk5 in
APP processing, and suggest that p35- and p25-mediated Cdk5
activities lead to discrete APP phosphorylation. | | | |
Interaction id | 74265 | |
MOLECULE A | |
Id | 8851 |
Type | Protein |
Species | Homo sapiens-e | |
Attribute |
--
|
Structure Details | -- |
Disease Details | -- | |
MOLECULE B | |
Id | 1020 |
Type | Protein |
Species | Homo sapiens | |
Attribute | -- |
Structure Details | -- |
Disease Details | -- | | Kinetics | - | |
|
General Information |
Interaction term | Increases activity (
direct ) | |
Pathway | | |
Interaction result | |
Other Resultant | | Leads to APP phosphorylation |
| |
Disease Details | | disease: :Alzheimer Disease |
| |
Experimental location and method | - species::Human
- cell::SHSY5Y cells
| |
Comments | |
Property | | Overexpressed p35 and truncated isoform p25 of CDK5R1 |
| |
References | |
PubMed Id | 12860412 | |
Author | Liu F, Su Y, Li B, Zhou Y, Ryder J, Gonzalez-DeWhitt P, May
PC, Ni B | |
Title | Regulation of amyloid precursor protein (APP) phosphorylation
and processing by p35/Cdk5 and p25/Cdk5. |
|
|
| | |
| 143408 | CDK5 | Protein | Homo sapiens-e | Phosphorylate | direct | MAPT | Protein | Homo sapiens | | | Hyperphosphorylated tau is a major component
of neurofibrillary tangles, one of the hallmarks of
Alzheimer's disease. / In this study, we have examined
the kinetic characteristics of in vitro phosphorylation of
the longest isoform of human tau by CDK5 and its activators
using recombinant proteins. Although the kinase activity of
CDK5 in phosphorylating tau was significantly higher in the
presence of p25, the affinity of CDK5 for tau was not
different. Phosphopeptide mapping revealed enhanced
phosphorylation of Ser(202)/Thr(205) residues by p25-CDK5
(amino acid residues of tau are numbered according to the
longest isoform of human tau). These results suggest that
cleavage of p35 to p25 greatly enhances the kinase activity
of CDK5 and increases the phosphorylation of Ser(202)/Thr(205). | | | |
Interaction id | 143408 | |
MOLECULE A | |
Id | 1020 |
Type | Protein |
Species | Homo sapiens-e | |
Attribute |
--
|
Structure Details | -- |
Disease Details | -- | |
MOLECULE B | |
Id | 4137 |
Type | Protein |
Species | Homo sapiens | |
Attribute | -- |
Structure Details | -- |
Disease Details | -- | |
Regulator | |
Regulation | Positive | | Description | p25 cleavage product of CDK5R1 |
|
| | Kinetics | - | |
|
General Information |
Interaction term | Phosphorylate (
direct ) | |
Pathway | Protein serine/threonine kinase
activity:cyclin-dependent protein kinaseCytoskeletal protein binding:MAPT (tau) associated | |
Disease Details | | disease: :Alzheimer Disease |
| |
Experimental location and method | - Experimental method::Peptide Mapping
| |
Comments | |
Property | | Variant form of molecule:MAPT(Longest isoform of MAPT) |
Domain_motif_site_residue | | [RES:Ser202;Thr205](4137) |
| |
References | |
PubMed Id | 12226093 | |
Author | Hashiguchi M, Saito T, Hisanaga S, Hashiguchi T | |
Title | Truncation of CDK5 activator p35 induces intensive
phosphorylation of Ser202/Thr205 of human tau. |
|
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