+ |
VPS4A | up-regulates activity
cleavage
|
CHMP2A |
0.909 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260846 |
|
|
in vitro |
|
pmid |
sentence |
30989108 |
Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
VPS4A | up-regulates activity
cleavage
|
CHMP3 |
0.645 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260847 |
|
|
in vitro |
|
pmid |
sentence |
30989108 |
Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission. |
|
Publications: |
1 |
Organism: |
In Vitro |