CoChat
Sign Up
PreprintCited by 22Cellular Mechanics and InteractionsProtein Structure and DynamicsCardiomyopathy and Myosin Studies

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

Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms

Open access
Selvaraj, Muniyandi, Kokate, Shrikant, Reggiano, Gabriella, Kogan, Konstantin, Kotila, Tommi, Kremneva, Elena, DiMaio, Frank, Lappalainen, Pekka, Huiskonen, Juha T.·2022·Cell Reports
DOI 10.1101/2022.05.12.491677

Preprint — published as 10.1016/j.celrep.2022.111900 · Paper page

Open this paper in CoChat — free account

Abstract

SUMMARY: The actin cytoskeleton is critical for cell migration, morphogenesis, endocytosis, organelle dynamics, and cytokinesis. To support diverse cellular processes, actin filaments form a variety of structures with specific architectures and dynamic properties. Key proteins specifying actin filaments are tropomyosins. Non-muscle cells express several functionally non-redundant tropomyosin isoforms, which differentially control the interactions of other proteins, including myosins and ADF/cofilin, with actin filaments. However, the underlying molecular mechanisms have remained elusive. By determining the cryogenic electron microscopy structures of actin filaments decorated by two functionally distinct non-muscle tropomyosin isoforms, Tpm1.6 and Tpm3.2, we reveal that actin filament conformation remains unaffected upon binding. However, Tpm1.6 and Tpm3.2 follow different paths along the major groove of the actin filament, providing an explanation for their incapability to co-polymerize on actin filaments. The structures and biochemical work also elucidate the molecular basis underlying specific roles of Tpm1.6 and Tpm3.2 in myosin II activation and protecting actin filaments from ADF/cofilin-catalysed severing.

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 · 10.1101/2022.05.12.491677

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. 10.1107/S2059798318006551 · DOI
  2. 10.1016/j.molcel.2006.08.006 · DOI
  3. 10.1128/MCB.00857-08 · DOI
  4. 10.1016/j.cell.2012.05.037 · DOI
  5. 10.1152/physrev.00018.2013 · DOI
  6. 2020, Diversity from similarity: cellular strategies for assigning particular identities to actin filaments and networks, Open Biology, 10, 200157, 10.1098/rsob.200157 · DOI
  7. 10.1091/mbc.E02-04-0244 · DOI
  8. Cagigas, M.L. , Bryce, N.S. , Ariotti, N. , Brayford, S. , Gunning, P.W. , and Hardeman, E.C. (2021). Correlative cryo-ET identifies actin/tropomyosin filaments that mediate cell-substrate adhesion in cancer cells and mechanosensitivity of cell proliferation. Nature materials. · DOI
  9. Carman, P.J. , Barrie, K.R. , and Dominguez, R. (2021). Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins. Journal of Biological Chemistry 297. · DOI
  10. 2020, Current developments in Coot for macromolecular model building of Electron Cryo-microscopy and Crystallographic Data, Protein Science, 29, 1055, 10.1002/pro.3791 · DOI
  11. 10.1073/pnas.1807028115 · DOI
  12. 10.7554/eLife.23152 · DOI
  13. 10.1002/pro.2389 · DOI
  14. 10.1242/jcs.069971 · DOI
  15. 10.1107/S2059798318002425 · DOI
  16. 2020, Cryo-EM and molecular docking shows myosin loop 4 contacts actin and tropomyosin on thin filaments, Biophysical Journal, 119, 821, 10.1016/j.bpj.2020.07.006 · DOI
  17. 10.1152/ajpcell.00450.2010 · DOI
  18. 10.1016/j.cub.2017.01.018 · DOI
  19. 2012, 4.13 thin filament regulation, Comprehensive Biophysics, 4, 251
  20. 10.1016/j.jmb.2006.08.033 · DOI
  21. 10.1242/jcs.165563 · DOI
  22. 10.1242/jcs.172502 · DOI
  23. 10.1016/j.jsb.2017.02.003 · DOI
  24. 10.1080/19490992.2016.1201619 · DOI
  25. 10.1091/mbc.E18-12-0815 · DOI
  26. 10.1016/j.cub.2014.05.034 · DOI
  27. 2020, Tropomodulins Control the Balance between Protrusive and Contractile Structures by Stabilizing Actin-Tropomyosin Filaments, Current Biology, 30, 767, 10.1016/j.cub.2019.12.049 · DOI
  28. 2019, The effect of tropomyosin mutations on actin-tropomyosin binding: in search of lost time, Biophysical Journal, 116, 2275, 10.1016/j.bpj.2019.05.009 · DOI
  29. 10.1016/j.bbrc.2014.02.097 · DOI
  30. Meiring, J. , Bryce, N.S. , Niño, J.L.G. , Gabriel, A. , Tay, S.S. , Hardeman, E. , Biro, M. , and Gunning, P. (2019a). Tropomyosin concentration but not formin nucleators mDia1 and mDia3 determines the level of tropomyosin incorporation into actin filaments. Scientific Reports 9. · DOI
  31. 2019, Tropomyosin concentration but not formin nucleators mDia1 and mDia3 determines the level of tropomyosin incorporation into actin filaments, Scientific reports, 9, 1
  32. 10.1083/jcb.200110013 · DOI
  33. 10.1074/jbc.M117.806521 · DOI
  34. 2020, Protein-protein docking reveals dynamic interactions of tropomyosin on actin filaments, Biophysical journal, 119, 75, 10.1016/j.bpj.2020.05.017 · DOI
  35. 10.1002/PRO.3943 · DOI
  36. 10.1074/jbc.M111.307330 · DOI
  37. 2021, High-resolution cryo-EM structure of the cardiac actomyosin complex, Structure, 29, 50, 10.1016/j.str.2020.09.013 · DOI
  38. 10.1016/j.jsb.2015.08.008 · DOI
  39. 10.1016/j.str.2013.08.005 · DOI
  40. 10.1016/j.cub.2011.03.064 · DOI · Paper page
  41. 10.1038/s41467-018-05046-2 · DOI
  42. 10.1016/j.cub.2011.03.007 · DOI
  43. 2015, Structure of the F-actin–tropomyosin complex, Nature, 519, 114, 10.1038/nature14033 · DOI
  44. 10.7554/eLife.17219 · DOI · Paper page
  45. 10.1093/nar/gky427 · DOI
  46. 10.1002/pro.3330 · DOI · Paper page
  47. 10.1016/j.cub.2017.05.048 · DOI
  48. 2020, Cardiac muscle thin filament structures reveal calcium regulatory mechanism, Nature communications, 11, 1
  49. 2017, MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy, Nature methods, 14, 331, 10.1038/nmeth.4193 · DOI
  50. 10.7554/eLife.42166 · DOI

Metadata

Authors
Selvaraj, M., Kokate, S., Reggiano, G., Kogan, K., Kotila, T., Kremneva, E., DiMaio, F., Lappalainen, P., & Huiskonen, J. T.
Affiliations
  • University of Helsinki (FI)
  • University of Washington (US)
Corresponding author
  • Lappalainen, Pekka
  • Huiskonen, Juha T.
ORCID
Venue
Cell Reports
Publisher
openRxiv
Published
2022-05-12
Volume
42
Issue
1
Pages
111900-111900
ISSN
2211-1247 (ISSN-L)
DOI
10.1101/2022.05.12.491677
OpenAlex
W4313379699
Cited by
22
References
1
Citations by year
2026: 4 · 2025: 8 · 2024: 7 · 2023: 3
FWCI
2.40
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Cell Reports (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • Työväentutkimus Vuosikirja (submittedVersion)
Funders
  • Helsingin Yliopisto
  • Academy of Finland (346133)
  • China Scholarship Council
  • Sigrid Juséliuksen Säätiö (4708344)
  • Biocenter Finland
  • Helsinki Institute of Life Science, Helsingin Yliopisto
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
Keywords
tropomyosin isoforms, actin filament structure, ADF/cofilin, actin filament severing, actin cytoskeleton
MeSH terms
Actins, Actin Cytoskeleton, Protein Binding, Tropomyosin, Protein Isoforms, Actin Depolymerizing Factors

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