| + |
CALM1 | up-regulates activity 
binding
|
KIF1A |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266888 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
To better understand how KIF1A-driven dense core vesicle (DCV) transport is regulated, we identified the KIF1A interactome and focused on three binding partners, the calcium binding protein calmodulin (CaM) and two synaptic scaffolding proteins: liprin-α and TANC2. We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility. We show that Ca2+/CaM-dependent modulation on KIF1A allows for binding to vesicular cargo. Our results indicate that at low calcium concentrations, the tail domain of KIF1A does not bind to vesicular cargo, whereas at high calcium concentrations, CaM binds KIF1A, allowing for subsequent DCV motility. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
KIF1A | up-regulates 
|
Dense-core_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266893 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 30021165 |
To better understand how KIF1A-driven dense core vesicle (DCV) transport is regulated, we identified the KIF1A interactome and focused on three binding partners, the calcium binding protein calmodulin (CaM) and two synaptic scaffolding proteins: liprin-α and TANC2. We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility. In contrast, liprin-α and TANC2 are not part of the KIF1A-cargo complex but capture DCVs at dendritic spines |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CALM3 | up-regulates activity
binding
|
KIF1A |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266890 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
To better understand how KIF1A-driven dense core vesicle (DCV) transport is regulated, we identified the KIF1A interactome and focused on three binding partners, the calcium binding protein calmodulin (CaM) and two synaptic scaffolding proteins: liprin-α and TANC2. We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility. In contrast, liprin-α and TANC2 are not part of the KIF1A-cargo complex but capture DCVs at dendritic spines. we can conclude that TANC2 and liprin-α are enriched in dendritic spines and interact with various synaptic proteins. TANC2 and Liprin-α2 Act as Immobile Postsynaptic Posts Able to Recruit KIF1A in a Subset of Dendritic Spines |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
Liprin-alpha | up-regulates activity
binding
|
KIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266892 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
Kinesin-3 Family Member KIF1A Interacts with Liprin-α and TANC2. TANC2 and Liprin-α Recruit KIF1A-Driven DCVs in Dendritic Spines. Upon Ca2+/CaM binding, KIF1A is activated, allowing for DCV loading and motility. KIF1A-driven DCVs are recruited in dendritic spines by liprin-α and TANC2, which ensure a precise mechanism of synaptic tagging for the vesicles. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
KIF1A | up-regulates
|
Plus-end directed sliding movement |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272522 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19773780 |
In general, N-kinesins and C-kinesins drive microtubule plus end- and minus end-directed motilities, respectively, and M-kinesins depolymerize microtubules1,9 (Box 1).|Forty-five genes that encode kinesin superfamily proteins (also known as KIFs) have been discovered in the mouse and human genomes.|KIFs are molecular motors that directionally transport various cargos, including membranous organelles, protein complexes and mRNAs, along the microtubule system. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM2 | up-regulates activity
binding
|
KIF1A |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266889 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
To better understand how KIF1A-driven dense core vesicle (DCV) transport is regulated, we identified the KIF1A interactome and focused on three binding partners, the calcium binding protein calmodulin (CaM) and two synaptic scaffolding proteins: liprin-α and TANC2. We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility. In contrast, liprin-α and TANC2 are not part of the KIF1A-cargo complex but capture DCVs at dendritic spines |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
TANC2 | up-regulates activity
binding
|
KIF1A |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266891 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
Kinesin-3 Family Member KIF1A Interacts with Liprin-α and TANC2. TANC2 and Liprin-α Recruit KIF1A-Driven DCVs in Dendritic Spines. Upon Ca2+/CaM binding, KIF1A is activated, allowing for DCV loading and motility. KIF1A-driven DCVs are recruited in dendritic spines by liprin-α and TANC2, which ensure a precise mechanism of synaptic tagging for the vesicles. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
KIF1A
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