Evidence map›Paper›PMID 22514729›Full record

ArticlePloS one2012

Lasp-1 regulates podosome function.

Miriam Stölting, Christiane Wiesner, Vanessa van Vliet, Elke Butt, Hermann Pavenstädt, Stefan Linder, Joachim Kremerskothen

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Loss of NSE-4 Perturbs Genome Stability and DNA Repair inInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. The Nebulin Family LIM and SH3 Proteins Regulate Postsynaptic Development and Function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors.

Miriam StöltingMedizinische Klinik D, Abteilung für Molekulare Nephrologie, Universitätsklinikum Münster, Münster, Germany.
Christiane Wiesner
Vanessa van Vliet
Elke Butt
Hermann Pavenstädt
Stefan Linder
Joachim Kremerskothen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins. Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulate cytoskeleton architecture and cell migration. This multidomain protein is predominantely present at focal adhesions, however, a second pool of Lasp-1 molecules is also found at lamellipodia and vesicle-like microdomains in the cytosol.In this report, we show that Lasp-1 is a novel component and regulator of podosomes. Immunofluorescence studies reveal a localization of Lasp-1 in the podosome ring structure, where it colocalizes with zyxin and vinculin. Life cell imaging experiments demonstrate that Lasp-1 is recruited in early steps of podosome assembly. A siRNA-mediated Lasp-1 knockdown in human macrophages affects podosome dynamics as well as their matrix degradation capacity. In summary, our data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell LineCells, CulturedCytoskeletal ProteinsCytoskeletonFocal AdhesionsHumansLIM Domain ProteinsMacrophagesMicrofilament ProteinsNerve Tissue ProteinsPseudopodiaRatsRNA, Small InterferingVinculinAdaptor Proteins, Signal TransducingCytoskeletal ProteinsLASP1 protein, humanLasp1 protein, ratLIM Domain ProteinsMicrofilament ProteinsNerve Tissue ProteinsRNA, Small InterferingVinculinZyxin

Identifiers

PMID22514729
PMCPMC3325968

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.