TY - JOUR
T1 - ATP-dependent force generation and membrane scission by ESCRT-III and Vps4
AU - Schöneberg, Johannes
AU - Pavlin, Mark Remec
AU - Yan, Shannon
AU - Righini, Maurizio
AU - Lee, Il Hyung
AU - Carlson, Lars Anders
AU - Bahrami, Amir Houshang
AU - Goldman, Daniel H.
AU - Ren, Xuefeng
AU - Hummer, Gerhard
AU - Bustamante, Carlos
AU - Hurley, James H.
N1 - Publisher Copyright:
© 2018 American Association for the Advancement of Science. All rights reserved.
PY - 2018/12/21
Y1 - 2018/12/21
N2 - The endosomal sorting complexes required for transport (ESCRTs) catalyze reverse-topology scission from the inner face of membrane necks in HIV budding, multivesicular endosome biogenesis, cytokinesis, and other pathways. We encapsulated ESCRT-III subunits Snf7, Vps24, and Vps2 and the AAA+ ATPase (adenosine triphosphatase) Vps4 in giant vesicles from which membrane nanotubes reflecting the correct topology of scission could be pulled. Upon ATP release by photo-uncaging, this system generated forces within the nanotubes that led to membrane scission in a manner dependent upon Vps4 catalytic activity and Vps4 coupling to the ESCRT-III proteins. Imaging of scission revealed Snf7 and Vps4 puncta within nanotubes whose presence followed ATP release, correlated with force generation and nanotube constriction, and preceded scission. These observations directly verify long-standing predictions that ATP-hydrolyzing assemblies of ESCRT-III and Vps4 sever membranes.
AB - The endosomal sorting complexes required for transport (ESCRTs) catalyze reverse-topology scission from the inner face of membrane necks in HIV budding, multivesicular endosome biogenesis, cytokinesis, and other pathways. We encapsulated ESCRT-III subunits Snf7, Vps24, and Vps2 and the AAA+ ATPase (adenosine triphosphatase) Vps4 in giant vesicles from which membrane nanotubes reflecting the correct topology of scission could be pulled. Upon ATP release by photo-uncaging, this system generated forces within the nanotubes that led to membrane scission in a manner dependent upon Vps4 catalytic activity and Vps4 coupling to the ESCRT-III proteins. Imaging of scission revealed Snf7 and Vps4 puncta within nanotubes whose presence followed ATP release, correlated with force generation and nanotube constriction, and preceded scission. These observations directly verify long-standing predictions that ATP-hydrolyzing assemblies of ESCRT-III and Vps4 sever membranes.
UR - http://www.scopus.com/inward/record.url?scp=85058811123&partnerID=8YFLogxK
U2 - 10.1126/science.aat1839
DO - 10.1126/science.aat1839
M3 - Article
C2 - 30573630
AN - SCOPUS:85058811123
SN - 0036-8075
VL - 362
SP - 1423
EP - 1428
JO - Science
JF - Science
IS - 6421
ER -
