| + |
OSBPL9-OSBPL10 oxysterol-binding protein-related complex | up-regulates quantity
relocalization
|
phosphatidyl-L-serine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281507 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36853333 |
We showed that the PH domains of ORP9 and ORP10 could interact with PI4P on the TGN, providing the membrane tethering to target TGN. This reconstitution system demonstrated that the ORP9-ORP10 complex efficiently transfers PI4P/PS between the apposed membranes. Previous studies showed that ORP10 maintains the ER-TGN MCSs integrity with the requirement of PS transfer from the ER to the TGN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OSBPL9 | form complex
binding
|
OSBPL9-OSBPL10 oxysterol-binding protein-related complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281504 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36853333 |
In this work, we discovered that ORP9 and ORP10 form a binary complex through intermolecular coiled-coil (CC) domain-CC domain interaction. The PH domains of ORP9 and ORP10 specially interact with phosphatidylinositol 4-phosphate (PI4P), mediating the TGN targeting. The ORP9-ORP10 complex plays a critical role in regulating PI4P levels at the TGN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OSBPL10 | form complex
binding
|
OSBPL9-OSBPL10 oxysterol-binding protein-related complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36853333 |
In this work, we discovered that ORP9 and ORP10 form a binary complex through intermolecular coiled-coil (CC) domain-CC domain interaction. The PH domains of ORP9 and ORP10 specially interact with phosphatidylinositol 4-phosphate (PI4P), mediating the TGN targeting. The ORP9-ORP10 complex plays a critical role in regulating PI4P levels at the TGN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OSBPL9-OSBPL10 oxysterol-binding protein-related complex | up-regulates quantity
relocalization
|
phosphatidylinositol 4-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281506 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36853333 |
We showed that the PH domains of ORP9 and ORP10 could interact with PI4P on the TGN, providing the membrane tethering to target TGN. This reconstitution system demonstrated that the ORP9-ORP10 complex efficiently transfers PI4P/PS between the apposed membranes. Previous studies showed that ORP10 maintains the ER-TGN MCSs integrity with the requirement of PS transfer from the ER to the TGN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |