Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly
© 2014 Shen et al..
The scission of biological membranes is facilitated by a variety of protein complexes that bind and manipulate lipid bilayers. ESCRT-III (endosomal sorting complex required for transport III) filaments mediate membrane scission during the ostensibly disparate processes of multivesicular endosome biogenesis, cytokinesis, and retroviral budding. However, mechanisms by which ESCRT-III subunits assemble into a polymer remain unknown. Using cryogenic electron microscopy (cryo-EM), we found that the full-length ESCRT-III subunit Vps32/CHMP4B spontaneously forms single-stranded spiral filaments. The resolution afforded by two-dimensional cryo-EM combined with molecular dynamics simulations revealed that individual Vps32/CHMP4B monomers within a filament are flexible and able to accommodate a range of bending angles. In contrast, the interface between monomers is stable and refractory to changes in conformation. We additionally found that the carboxyl terminus of Vps32/CHMP4B plays a key role in restricting the lateral association of filaments. Our findings highlight new mechanisms by which ESCRT-III filaments assemble to generate a unique polymer capable of membrane remodeling in multiple cellular contexts.
Medienart: |
E-Artikel |
---|
Erscheinungsjahr: |
2014 |
---|---|
Erschienen: |
2014 |
Enthalten in: |
Zur Gesamtaufnahme - volume:206 |
---|---|
Enthalten in: |
The Journal of cell biology - 206(2014), 6 vom: 15. Sept., Seite 763-77 |
Sprache: |
Englisch |
---|
Beteiligte Personen: |
Shen, Qing-Tao [VerfasserIn] |
---|
Links: |
---|
Themen: |
Endosomal Sorting Complexes Required for Transport |
---|
Anmerkungen: |
Date Completed 18.11.2014 Date Revised 21.10.2021 published: Print-Electronic PDB: 2GD5 Citation Status MEDLINE |
---|
doi: |
10.1083/jcb.201403108 |
---|
funding: |
|
---|---|
Förderinstitution / Projekttitel: |
|
PPN (Katalog-ID): |
NLM241719240 |
---|
LEADER | 01000naa a22002652 4500 | ||
---|---|---|---|
001 | NLM241719240 | ||
003 | DE-627 | ||
005 | 20231224124847.0 | ||
007 | cr uuu---uuuuu | ||
008 | 231224s2014 xx |||||o 00| ||eng c | ||
024 | 7 | |a 10.1083/jcb.201403108 |2 doi | |
028 | 5 | 2 | |a pubmed24n0805.xml |
035 | |a (DE-627)NLM241719240 | ||
035 | |a (NLM)25202029 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
100 | 1 | |a Shen, Qing-Tao |e verfasserin |4 aut | |
245 | 1 | 0 | |a Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly |
264 | 1 | |c 2014 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ƒaComputermedien |b c |2 rdamedia | ||
338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
500 | |a Date Completed 18.11.2014 | ||
500 | |a Date Revised 21.10.2021 | ||
500 | |a published: Print-Electronic | ||
500 | |a PDB: 2GD5 | ||
500 | |a Citation Status MEDLINE | ||
520 | |a © 2014 Shen et al. | ||
520 | |a The scission of biological membranes is facilitated by a variety of protein complexes that bind and manipulate lipid bilayers. ESCRT-III (endosomal sorting complex required for transport III) filaments mediate membrane scission during the ostensibly disparate processes of multivesicular endosome biogenesis, cytokinesis, and retroviral budding. However, mechanisms by which ESCRT-III subunits assemble into a polymer remain unknown. Using cryogenic electron microscopy (cryo-EM), we found that the full-length ESCRT-III subunit Vps32/CHMP4B spontaneously forms single-stranded spiral filaments. The resolution afforded by two-dimensional cryo-EM combined with molecular dynamics simulations revealed that individual Vps32/CHMP4B monomers within a filament are flexible and able to accommodate a range of bending angles. In contrast, the interface between monomers is stable and refractory to changes in conformation. We additionally found that the carboxyl terminus of Vps32/CHMP4B plays a key role in restricting the lateral association of filaments. Our findings highlight new mechanisms by which ESCRT-III filaments assemble to generate a unique polymer capable of membrane remodeling in multiple cellular contexts | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, N.I.H., Extramural | |
650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
650 | 7 | |a Endosomal Sorting Complexes Required for Transport |2 NLM | |
650 | 7 | |a Polymers |2 NLM | |
650 | 7 | |a Protein Subunits |2 NLM | |
700 | 1 | |a Schuh, Amber L |e verfasserin |4 aut | |
700 | 1 | |a Zheng, Yuqing |e verfasserin |4 aut | |
700 | 1 | |a Quinney, Kyle |e verfasserin |4 aut | |
700 | 1 | |a Wang, Lei |e verfasserin |4 aut | |
700 | 1 | |a Hanna, Michael |e verfasserin |4 aut | |
700 | 1 | |a Mitchell, Julie C |e verfasserin |4 aut | |
700 | 1 | |a Otegui, Marisa S |e verfasserin |4 aut | |
700 | 1 | |a Ahlquist, Paul |e verfasserin |4 aut | |
700 | 1 | |a Cui, Qiang |e verfasserin |4 aut | |
700 | 1 | |a Audhya, Anjon |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t The Journal of cell biology |d 1962 |g 206(2014), 6 vom: 15. Sept., Seite 763-77 |w (DE-627)NLM000005266 |x 1540-8140 |7 nnns |
773 | 1 | 8 | |g volume:206 |g year:2014 |g number:6 |g day:15 |g month:09 |g pages:763-77 |
856 | 4 | 0 | |u http://dx.doi.org/10.1083/jcb.201403108 |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a GBV_NLM | ||
951 | |a AR | ||
952 | |d 206 |j 2014 |e 6 |b 15 |c 09 |h 763-77 |