Evidence map›Paper›PMID 22665060›Full record

ArticleOncogene2013

Nuclear import of LASP-1 is regulated by phosphorylation and dynamic protein-protein interactions.

S Mihlan, C Reiß, P Thalheimer, S Herterich, S Gaetzner, J Kremerskothen, H J Pavenstädt, U Lewandrowski, A Sickmann, E Butt

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. 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
  14. Article
  15. An emerging link between LIM domain proteins and nuclear receptors.Cellular and molecular life sciences : CMLS · 2018
    Review
  16. Article
  17. Review
  18. Article
  19. Analyses of PDE-regulated phosphoproteomes reveal unique and specific cAMP-signaling modules in T cells.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017
    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

10 authors at 2 institutions in 1 country.

S MihlanInstitute of Clinical Biochemistry and Pathobiochemistry, University Clinic of Wuerzburg, Wuerzburg, Germany.
C Reiß
P Thalheimer
S Herterich
S Gaetzner
J Kremerskothen
H J Pavenstädt
U Lewandrowski
A Sickmann
E Butt
Leibniz Institute for Analytical Sciences - ISAS · DEUniversity Hospital Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LASP-1 is a multidomain protein predominantly localized at focal contacts, where it regulates cytoskeleton dynamics and cell migration. However, in different tumor entities, a nuclear LASP-1 accumulation is observed, thought to have an important role in cancer progression. Until now, the molecular mechanisms that control LASP-1 nuclear import were not elucidated. Here, we identified a novel LASP-1-binding partner, zona occludens protein 2 (ZO-2), and established its role in the signal transduction pathway of LASP-1 nucleo-cytoplasmatic shuttling. Phosphorylation of LASP-1 by PKA at serine 146 induces translocation of the LASP-1/ZO-2 complex from the cytoplasm to the nucleus. Interaction occurs within the carboxyterminal proline-rich motif of ZO-2 and the SH3 domain in LASP-1. In situ proximity ligation assay confirmed the direct binding between LASP-1 and ZO-2 and visualized the shuttling. Nuclear export is mediated by Crm-1 and a newly identified nuclear export signal in LASP-1. Finally, dephosphorylation of LASP-1 by phosphatase PP2B is suggested to relocalize the protein back to focal contacts. In summary, we define a new pathway for LASP-1 in tumor progression.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingBreast NeoplasmsCell Line, TumorCell NucleusCyclic AMP-Dependent Protein KinasesCytoskeletal ProteinsHumansLIM Domain ProteinsPhosphorylationProtein BindingProtein Structure, TertiarySignal TransductionZonula Occludens-2 ProteinAdaptor Proteins, Signal TransducingCyclic AMP-Dependent Protein KinasesCytoskeletal ProteinsLASP1 protein, humanLIM Domain ProteinsTJP2 protein, humanZonula Occludens-2 Protein

Identifiers

PMID22665060
OpenAlexW1983421902

What OpenQuestion holds

Textmetadata
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.