+ |
APBA1 | up-regulates activity
binding
|
NRXN1 |
0.653 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264038 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11036064 |
Mint1 and Mint2 Interact with the Cytoplasmic Domain of Neurexin I. The interaction of Mint1 with neurexins is mediated by its PDZ domains and allows the formation of mixed CASK-Mint complexes. Both CASK and Mint1 can bind directly to neurexins and to each other. Therefore, the assembly of various multimeric complexes could proceed as CASK could be indirectly recruited to neurexin-bound Mint1 and vice versa. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
Pathways: | Neurotransmitters release |
+ |
APBA1 | up-regulates activity
binding
|
CASK |
0.846 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264041 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
11036064 |
Interaction with Munc18 increases Mint1 binding to CASK. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
APBA1 | up-regulates activity
binding
|
STXBP1 |
0.689 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264035 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
9395480 |
Munc18-1 is a neuronal protein that interacts with syntaxin 1 and is required for synaptic vesicle exocytosis. We have now identified two Munc18-1-interacting proteins called Mint1 and Mint2 that may mediate the function of Munc18-1. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Pathways: | Neurotransmitters release |
+ |
APBA1 | up-regulates
|
Exocytosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264043 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
11036064 |
As neurexins have been proposed to function in neuronal cell adhesion, it is possible that they define specific sites at the plasma membrane and that Mint complexes and Mint1-CASK complexes on neurexin are involved in the localized recruitment of Munc18 to the sites of exocytosis. In support of this hypothesis, both CASK and Mint1 have been reported to be localized at synapses |
|
Publications: |
1 |
Organism: |
Homo Sapiens |