Evidence map›Paper›PMID 33568673›Full record

ArticleNature communications2021

Quantitative single-protein imaging reveals molecular complex formation of integrin, talin, and kindlin during cell adhesion.

Lisa S Fischer, Christoph Klingner, Thomas Schlichthaerle, Maximilian T Strauss, Ralph Böttcher, Reinhard Fässler, Ralf Jungmann, Carsten Grashoff

Abstract readEvaluation Study
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed.

  1. Review
  2. Quantitative nanoscale imaging shows peptide-MHC I complexes are monomeric and spatially regulated in human dendritic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cryosectioning-enhanced super-resolution microscopy for single-protein imaging across cells and tissues.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Cluster parameter-based DBSCAN maps for image characterization.Computational and structural biotechnology journal · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Lisa S Fischer *Department of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, Münster, Germany.ORCID 0000-0002-3113-1236
Christoph Klingner *Department of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, Münster, Germany.
Thomas Schlichthaerle *Faculty of Physics and Center for Nanoscience, LMU Munich, Munich, Germany.
Maximilian T StraussFaculty of Physics and Center for Nanoscience, LMU Munich, Munich, Germany.ORCID 0000-0003-3320-6833
Ralph BöttcherDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0003-3050-7163
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany. faessler@biochem.mpg.de.ORCID 0000-0002-0145-6937
Ralf JungmannFaculty of Physics and Center for Nanoscience, LMU Munich, Munich, Germany. jungmann@biochem.mpg.de.ORCID 0000-0003-4607-3312
Carsten GrashoffDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, Münster, Germany. grashoff@wwu.de.ORCID 0000-0003-0118-9231

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule localization microscopy (SMLM) enabling the investigation of individual proteins on molecular scales has revolutionized how biological processes are analysed in cells. However, a major limitation of imaging techniques reaching single-protein resolution is the incomplete and often unknown labeling and detection efficiency of the utilized molecular probes. As a result, fundamental processes such as complex formation of distinct molecular species cannot be reliably quantified. Here, we establish a super-resolution microscopy framework, called quantitative single-molecule colocalization analysis (qSMCL), which permits the identification of absolute molecular quantities and thus the investigation of molecular-scale processes inside cells. The method combines multiplexed single-protein resolution imaging, automated cluster detection, in silico data simulation procedures, and widely applicable experimental controls to determine absolute fractions and spatial coordinates of interacting species on a true molecular level, even in highly crowded subcellular structures. The first application of this framework allowed the identification of a long-sought ternary adhesion complex-consisting of talin, kindlin and active β1-integrin-that specifically forms in cell-matrix adhesion sites. Together, the experiments demonstrate that qSMCL allows an absolute quantification of multiplexed SMLM data and thus should be useful for investigating molecular mechanisms underlying numerous processes in cells.

Indexed as

AnimalsCell AdhesionCell LineCytoskeletal ProteinsHumansIntegrin beta1MiceMuscle ProteinsSingle Molecule ImagingTalinCytoskeletal ProteinsIntegrin beta1kindlin-2 protein, mouseMuscle ProteinsTalinTLN1 protein, human

Identifiers

PMID33568673
PMCPMC7876120

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.