+ |
STK38 | up-regulates activity
phosphorylation
|
AAK1 |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263034 |
Ser637 |
AGHRRILsDVTHSAV |
Mus musculus |
|
pmid |
sentence |
22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. AAK1 phosphorylation regulates dendrite branching and length |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Brain |
+ |
AAK1 | up-regulates
phosphorylation
|
NUMB |
0.472 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179606 |
Thr102 |
LRVVDEKtKDLIVDQ |
Homo sapiens |
|
pmid |
sentence |
18657069 |
Collectively, these observations demonstrate that numb endocytic activity is regulated by aak1 and that phosphorylation may be a critical step in promoting coated pit maturation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AAK1 |
phosphorylation
|
NUMB |
0.472 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179610 |
Thr102 |
LRVVDEKtKDLIVDQ |
Homo sapiens |
|
pmid |
sentence |
18657069 |
Numb is phosphorylated by aak1, while little aak1-dependent phosphorylation is observed in t102a numb immunoprecipitants |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AAK1 | up-regulates
phosphorylation
|
AP1M1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115589 |
Thr144 |
QEGHKLEtGAPRPPA |
Homo sapiens |
Neuron |
pmid |
sentence |
11877461 |
Aak1 is enriched at presynaptic terminals, whereas in nonneuronal cells it colocalizes with clathrin and ap2 in clathrin-coated pits and at the leading edge of migrating cells. Aak1 specifically phosphorylates the mu subunit in vitro, and stage-specific assays for endocytosis show that mu phosphorylation by aak1 results in a decrease in ap2-stimulated transferrin internalization. Together, these results provide strong evidence that aak1 is the endogenous mu 2 kinase and plays a regulatory role in clathrin-mediated endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AAK1 | up-regulates
phosphorylation
|
AP2M1 |
0.781 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115657 |
Thr156 |
SQITSQVtGQIGWRR |
Homo sapiens |
Neuron |
pmid |
sentence |
11877461 |
Aak1 is enriched at presynaptic terminals, whereas in nonneuronal cells it colocalizes with clathrin and ap2 in clathrin-coated pits and at the leading edge of migrating cells. Aak1 specifically phosphorylates the mu subunit in vitro, and stage-specific assays for endocytosis show that mu phosphorylation by aak1 results in a decrease in ap2-stimulated transferrin internalization. Together, these results provide strong evidence that aak1 is the endogenous mu 2 kinase and plays a regulatory role in clathrin-mediated endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AP-2 complex | up-regulates activity
binding
|
AAK1 |
0.64 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260393 |
|
|
Rattus norvegicus |
Brain |
pmid |
sentence |
15496985 |
We therefore characterised protein ligands using liquid chromatography tandem mass spectrometry (LC‐MS/MS) and confirmed this using Western blotting to recognise both major and minor bands. Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |