| + |
VAC14 | up-regulates quantity by stabilization 
binding
|
FIG4 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253534 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 20630877 |
Our data indentify a novel regulatory mechanism whereby ArPIKfyve enhances Sac3 abundance by attenuating Sac3 proteasome-dependent degradation and suggest that a failure of this mechanism could be the primary molecular defect in the pathogenesis of CMT4J. our data are consistent with the notion that when associated with ArPIKfyve, Sac3 is stabilized and protected from degradation, whereas in the absence of associated ArPIKfyve, Sac3 remains unfolded and, hence, prone to rapid destruction. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VAC14 | form complex 
binding
|
PAS complex |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253530 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17556371 |
Here we have identified and characterized Sac3, a Sac domain phosphatase, as the Fig4 mammalian counterpart. Endogenous Sac3, a widespread 97-kDa protein, formed a stable ternary complex with ArPIKfyve and PIKfyve. Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NBEAL2 |
binding
|
VAC14 |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261892 |
|
|
Mus musculus |
Blood Platelet |
| pmid |
sentence |
| 29187380 |
In summary, from 129 binding partners of Nbeal2 identified by mass spectrometry, we have confirmed the interaction of 3, Dock7, Sec16a, and Vac14, by different biochemical and cellular approaches|Given the significant reduction of Dock7 levels and its altered localization in Nbeal2−/− platelets, we postulated that this canonical signaling pathway may be disrupted and set out to test this using control and Nbeal2−/− platelets. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
VAC14
- 
- 