---
_id: '10369'
abstract:
- lang: eng
text: Biological membranes have a central role in mediating the organization of
membrane-curving proteins, a dynamic process that has proven to be challenging
to probe experimentally. Using atomic force microscopy, we capture the hierarchically
organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid
membranes. Their structure reveals distinct long linear aggregates of proteins,
regularly spaced by up to 300 nm. Employing accurate free-energy calculations
from large-scale coarse-grained computer simulations, we found that the membrane
mediates the interaction among protein filaments as a combination of short- and
long-ranged interactions. The long-ranged component acts at strikingly long distances,
giving rise to a variety of micron-sized ordered patterns. This mechanism may
contribute to the long-ranged spatiotemporal control of membrane remodeling by
proteins in the cell.
acknowledgement: M.S. and G.A.V. acknowledge their research reported in this publication
as being supported by the National Institute of General Medical Sciences of the
National Institutes of Health under Award Number R01-GM063796. Computational resources
were provided to M.S. and G.A.V. by the National Science Foundation through XSEDE
(Grant TG-MCA94P017, supercomputers Stampede and Gordon), and also by the Blue Waters
computing project at the National Center for Supercomputing Applications (University
of Illinois at Urbana–Champaign, NSF Awards OCI-0725070 and ACI-1238993). A.Š. acknowledges
support from the Human Frontier Science Program and Royal Society. J.M.H. and K.Y.C.L.
acknowledge the support from the National Science Foundation (Grant MCB-1413613)
and the NSF-supported MRSEC program at the University of Chicago (Grant DMR-1420709).
We are grateful to Carsten Mim and Vinzenz Unger of Northwestern University for
generously providing us with the protein. We thank all the members of the Voth group
for fruitful discussions, especially John M. A. Grime.
article_processing_charge: No
article_type: original
author:
- first_name: Mijo
full_name: Simunovic, Mijo
last_name: Simunovic
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: J. Michael
full_name: Henderson, J. Michael
last_name: Henderson
- first_name: Ka Yee C.
full_name: Lee, Ka Yee C.
last_name: Lee
- first_name: Gregory A.
full_name: Voth, Gregory A.
last_name: Voth
citation:
ama: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. Long-range organization
of membrane-curving proteins. ACS Central Science. 2017;3(12):1246-1253.
doi:10.1021/acscentsci.7b00392
apa: Simunovic, M., Šarić, A., Henderson, J. M., Lee, K. Y. C., & Voth, G. A.
(2017). Long-range organization of membrane-curving proteins. ACS Central Science.
American Chemical Society. https://doi.org/10.1021/acscentsci.7b00392
chicago: Simunovic, Mijo, Anđela Šarić, J. Michael Henderson, Ka Yee C. Lee, and
Gregory A. Voth. “Long-Range Organization of Membrane-Curving Proteins.” ACS
Central Science. American Chemical Society, 2017. https://doi.org/10.1021/acscentsci.7b00392.
ieee: M. Simunovic, A. Šarić, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range
organization of membrane-curving proteins,” ACS Central Science, vol. 3,
no. 12. American Chemical Society, pp. 1246–1253, 2017.
ista: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. 2017. Long-range organization
of membrane-curving proteins. ACS Central Science. 3(12), 1246–1253.
mla: Simunovic, Mijo, et al. “Long-Range Organization of Membrane-Curving Proteins.”
ACS Central Science, vol. 3, no. 12, American Chemical Society, 2017, pp.
1246–53, doi:10.1021/acscentsci.7b00392.
short: M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central
Science 3 (2017) 1246–1253.
date_created: 2021-11-29T08:49:50Z
date_published: 2017-11-21T00:00:00Z
date_updated: 2021-11-29T09:28:06Z
day: '21'
ddc:
- '540'
doi: 10.1021/acscentsci.7b00392
extern: '1'
external_id:
pmid:
- '29296664'
file:
- access_level: open_access
checksum: 1cf3e5e5342f2d728f47560acc3ec560
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-29T09:00:40Z
date_updated: 2021-11-29T09:00:40Z
file_id: '10371'
file_name: 2017_ACSCentSci_Simunovic.pdf
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relation: main_file
success: 1
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has_accepted_license: '1'
intvolume: ' 3'
issue: '12'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://pubs.acs.org/doi/10.1021/acscentsci.7b00392
month: '11'
oa: 1
oa_version: Published Version
page: 1246-1253
pmid: 1
publication: ACS Central Science
publication_identifier:
eissn:
- 2374-7951
issn:
- 2374-7943
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Long-range organization of membrane-curving proteins
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 3
year: '2017'
...