Evidence map›Paper›PMID 23389630›Full record

ArticleMolecular biology of the cell2013

Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.

Katherine T Bliss, Miensheng Chu, Colin M Jones-Weinert, Carol C Gregorio

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Bioinformatics Profiling and Experimental Validation of 4 Differentially-Expressed LIM Genes in the Course of Colorectal-Adenoma-Carcinoma.Medical science monitor : international medical journal of experimental and clinical research · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Review
  9. Quantitative Trait Module-Based Genetic Analysis of Alzheimer's Disease.International journal of molecular sciences · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
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

4 authors at 1 institution in 1 country.

Katherine T BlissDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, AZ 85724, USA.
Miensheng Chu
Colin M Jones-Weinert
Carol C Gregorio
University of Arizona · US

Funding

PHYSIOLOGYT32HL007249 · NHLBI · UNIVERSITY OF ARIZONA · PI Brett A Colson, JOHN P KONHILAS · 1985 to 2026
$12.5M
Deciphering the Roles of Nebulin in Cardiac Myofibril AssemblyR01HL083146 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2007 to 2011
$2.1M
Deciphering the role of the RNA-binding protein, FXR1, in cardiac muscle assemblyR01HL108625 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2012 to 2015
$1.9M
NHLBI NIH HHS HL083146NHLBI NIH HHS HL108625NHLBI NIH HHS R01 HL083146NHLBI NIH HHS R01 HL108625NHLBI NIH HHS T32 HL007249NHLBI NIH HHS T32 HL07249PHS HHS HHMI52005889
6 · The paper itself

Abstract

Focal adhesions are intricate protein complexes that facilitate cell attachment, migration, and cellular communication. Lasp-2 (LIM-nebulette), a member of the nebulin family of actin-binding proteins, is a newly identified component of these complexes. To gain further insights into the functional role of lasp-2, we identified two additional binding partners of lasp-2: the integral focal adhesion proteins vinculin and paxillin. Of interest, the interaction of lasp-2 with its binding partners vinculin and paxillin is significantly reduced in the presence of lasp-1, another nebulin family member. The presence of lasp-2 appears to enhance the interaction of vinculin and paxillin with each other; however, as with the interaction of lasp-2 with vinculin or paxillin, this effect is greatly diminished in the presence of excess lasp-1. This suggests that the interplay between lasp-2 and lasp-1 could be an adhesion regulatory mechanism. Lasp-2's potential role in metastasis is revealed, as overexpression of lasp-2 in either SW620 or PC-3B1 cells-metastatic cancer cell lines-increases cell migration but impedes cell invasion, suggesting that the enhanced interaction of vinculin and paxillin may functionally destabilize focal adhesion composition. Taken together, these data suggest that lasp-2 has an important role in coordinating and regulating the composition and dynamics of focal adhesions.

Indexed as

Cell MovementAdaptor Proteins, Signal TransducingBlotting, WesternCarrier ProteinsCell AdhesionCell Line, TumorCytoskeletal ProteinsGreen Fluorescent ProteinsHEK293 CellsHumansLIM Domain ProteinsMicroscopy, FluorescencePaxillinProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceAdaptor Proteins, Signal TransducingCarrier ProteinsCytoskeletal ProteinsGreen Fluorescent ProteinsLASP1 protein, humanLIM Domain ProteinsNEBL protein, humanPaxillinVinculin

Identifiers

PMID23389630
PMCPMC3608507
OpenAlexW2110626627

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.