CoChat
Sign Up
PreprintCited by 12Force Microscopy Techniques and ApplicationsProtein Structure and DynamicsDrug Transport and Resistance Mechanisms

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Probing the stability and interdomain interactions in the ABC transporter OpuA, using single-molecule optical tweezers

Open access
van der Sleen, Lyan, Stevens, Jan, Marrink, Siewert J., Poolman, Bert, Tych, Kasia·2023·Cell Reports
DOI 10.1101/2023.09.01.555951

Preprint — published as 10.1016/j.celrep.2024.114110 · Paper page

Open this paper in CoChat — free account

Abstract

Summary: Transmembrane transporter proteins are essential for the maintenance of cellular homeostasis and, as such, are key drug targets. Many transmembrane transporter proteins are known to undergo large structural rearrangements during their functional cycles. Despite the large amount of detailed structural and functional data available for these systems, our understanding of their dynamics and therefore how they function is generally limited. We introduce an innovative approach which enables us to directly measure the dynamics and stabilities of inter-domain interactions of transmembrane proteins using optical tweezers. Focusing on the osmoregulatory ABC transporter OpuA from Lactococcus lactis , we examine the mechanical properties and potential interactions of its substrate-binding domains. Our measurements are performed in lipid nanodiscs, providing a native-mimicking environment for the transmembrane protein. The technique provides high spatial and temporal resolution and allows us to study the functionally-relevant motions and inter-domain interactions of individual transmembrane transporter proteins in real-time in a lipid bilayer.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/2023.09.01.555951

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 50

  1. 10.1038/s43586-021-00021-6 · DOI
  2. 10.1140/epjp/s13360-020-00907-6 · DOI
  3. 10.1146/annurev-biochem-013118-111442 · DOI
  4. 10.1016/j.jmb.2021.167207 · DOI
  5. 10.1073/pnas.1107736109 · DOI
  6. 10.1038/nature09021 · DOI
  7. 10.1126/science.1116702 · DOI
  8. 10.1126/science.1207598 · DOI · Paper page
  9. 10.1038/s41467-023-36701-y · DOI
  10. 10.1038/ncomms10848 · DOI
  11. 10.1016/j.str.2017.11.023 · DOI
  12. 10.1073/pnas.1414073111 · DOI
  13. 10.1038/s41589-018-0025-4 · DOI
  14. 10.1101/2023.01.15.524119 · DOI
  15. 10.7554/eLife.85882 · DOI
  16. 10.1042/BST20180147 · DOI
  17. 10.1016/S1095-6433(01)00442-1 · DOI
  18. 10.1146/annurev-micro-090110-102815 · DOI · Paper page
  19. 10.1016/j.febslet.2005.11.079 · DOI
  20. 10.1073/pnas.0603871103 · DOI
  21. 10.1126/sciadv.abd7697 · DOI
  22. 10.1371/journal.pone.0010361 · DOI
  23. 10.1074/jbc.M304796200 · DOI
  24. 10.1074/jbc.M113.499327 · DOI
  25. 10.1074/jbc.M604907200 · DOI
  26. 10.1073/pnas.97.13.7102 · DOI
  27. 10.1093/emboj/20.24.7022 · DOI
  28. 10.1101/2023.07.13.548808 · DOI
  29. 10.1016/j.febslet.2009.10.024 · DOI
  30. 10.1016/j.sbi.2010.05.005 · DOI
  31. 10.1038/s41598-019-46525-w · DOI
  32. 10.1039/c7cp03327c · DOI
  33. 10.1016/j.jmb.2009.08.066 · DOI
  34. 10.1073/pnas.1504625112 · DOI
  35. 10.1038/s41467-019-11518-w · DOI
  36. 10.1073/pnas.0606236103 · DOI
  37. 10.1016/j.bpc.2011.05.012 · DOI
  38. 10.1016/S0076-6879(09)64011-8 · DOI
  39. 10.1007/s003390051103 · DOI
  40. 10.1016/j.softx.2015.06.001 · DOI · Paper page
  41. 10.1021/ct300400x · DOI
  42. 10.1021/ct700200b · DOI
  43. 10.1063/1.2408420 · DOI
  44. 10.1063/1.328693 · DOI
  45. 10.1063/1.464397 · DOI
  46. 10.1038/s41592-022-01488-1 · DOI · Paper page
  47. 10.1016/S0006-3495(02)75658-0 · DOI
  48. 10.1016/j.sbi.2019.12.015 · DOI
  49. 10.1021/acs.jctc.2c00498 · DOI
  50. 10.1038/s41592-019-0686-2 · DOI · Paper page

Metadata

Authors
van der Sleen, L., Stevens, J., Marrink, S. J., Poolman, B., & Tych, K.
Affiliations
University of Groningen (NL)
Corresponding author
Poolman, Bert
ORCID
Venue
Cell Reports
Publisher
openRxiv
Published
2023-09-05
Volume
43
Issue
4
Pages
114110-114110
ISSN
2211-1247 (ISSN-L)
DOI
10.1101/2023.09.01.555951
OpenAlex
W4394728395
Cited by
12
References
1
Citations by year
2026: 5 · 2025: 5 · 2024: 1 · 2023: 1
FWCI
1.74
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Cell Reports (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • SSRN Electronic Journal (acceptedVersion)
  • PubMed (publishedVersion)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Nederlandse Organisatie voor Wetenschappelijk Onderzoek (OCENW.KLEIN.526, NWA.1292.19.170)
Topics
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
OpuA, ABC transporters, domain-domain interactions, protein stability, substrate-binding domain, osmoregulation, Lactococcus lactis, lipid nanodiscs, single-molecule force spectroscopy, optical tweezers, protein mechanical properties
MeSH terms
Protein Domains, Single Molecule Imaging, Bacterial Proteins, Lipid Bilayers, Protein Binding, Lactococcus lactis, ATP-Binding Cassette Transporters, Optical Tweezers, Protein Stability

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review