| + |
VPS36 | form complex 
binding
|
ESCRT-II complex |
0.963 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280915 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18539118 |
ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. . Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNF8 | form complex
binding
|
ESCRT-II complex |
0.966 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280916 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18539118 |
ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. . Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-I complex, VPS37A-UBAP1 variant | up-regulates quantity 
binding
|
ESCRT-II complex |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280932 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
At the opposite end of the ESCRT-I rod, Vps28 binds to the GLUE domain of the ESCRT-II protein Vps36/Eap45 and thereby interacts with the ESCRT-II complex. In addition to cargo sorting, ESCRT-I together with ESCRT-II is capable of budding membranes into the lumen of giant unilamellar vesicles. The rigid architecture and size of ESCRT-I and ESCRT-II (see below) may help to stabilize the bud neck of a growing vesicle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-II complex | up-regulates quantity
binding
|
ESCRT-III |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280933 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
While cargo is collected, ESCRT-I together with ESCRT-II could initiate the budding process of the endosomal membrane. At the same time, both arms of ESCRT-II (Vps25/Eap20) could already interact with one copy of the first ESCRT-III subunit, Vps20/CHMP6 (charged multi-vesicular body protein 6), and convert it into an active nucleator for ESCRT-III assembly on endosomes.In contrast to the early ESCRT complexes (ESCRT-0, -I and -II), which form stable protein complexes in the cytoplasm, the ESCRT-III complex only transiently assembles on endosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-II complex | up-regulates 
|
Membrane_fusion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
In vivo and in vitro data suggest a key role for the ESCRT-III complex in all ESCRT-mediated membrane remodeling (budding and scission) reactions, although the mechanism is not understood. Hence, ESCRT-III filaments may have a dual role during MVB sorting: cargo sequestration within the site of MVB vesicle formation and membrane budding/scission. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS25 | form complex
binding
|
ESCRT-II complex |
0.959 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280917 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18539118 |
ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. . Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-II complex | up-regulates
|
Multivesicular_body_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280936 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
In vivo and in vitro data suggest a key role for the ESCRT-III complex in all ESCRT-mediated membrane remodeling (budding and scission) reactions, although the mechanism is not understood. Hence, ESCRT-III filaments may have a dual role during MVB sorting: cargo sequestration within the site of MVB vesicle formation and membrane budding/scission. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
ESCRT-II complex
CPX-2506