Evidence map›Paper›PMID 30704758›Full record

ArticleBiochemical and biophysical research communications2019

RECK isoforms differentially regulate fibroblast migration by modulating tubulin post-translational modifications.

Ha Neul Lee, Oye A Bosompra, Hilary A Coller

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
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  5. TwoGenes · 2021
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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

3 authors at 1 institution in 1 country.

Ha Neul LeeMolecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, 90095, USA.
Oye A BosompraDepartment of Molecular, Cell and Developmental Biology, University of California, Los Angeles, Los Angeles, CA, 90095, USA.
Hilary A CollerMolecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, 90095, USA; Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, Los Angeles, CA, 90095, USA; Department of Biological Chemistry, David Geffen School of Medicine, Los Angeles, Los Angeles, CA, 90095, USA. Electronic address: hcoller@ucla.edu.
University of California, Los Angeles · US

Funding

UCLA Clinical Translational Science InstituteUL1TR001881 · NCATS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ARLEEN F. BROWN, ARASH NAEIM · 2016 to 2026
$118.1M
UCLA Clinical and Translational Science InstituteUL1TR000124 · NCATS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DUBINETT, STEVEN M. · 2012 to 2015
$57.0M
Metabolic Control of Hair Follicle Stem Cell Homeostasis and TumorigenesisR01AR070245 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHRISTOFK, HEATHER, LOWRY, WILLIAM E · 2018 to 2022
$2.1M
The Role of MicroRNAs in Cellular QuiescenceR01GM081686 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COLLER, HILARY A · 2008 to 2012
$1.4M
A Combined Computational and Experimental Approach to Defining Mechanisms of micrR01GM086465 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COLLER, HILARY A · 2009 to 2012
$1.1M
Role of Tumor and Stromal Cell Metabolism in Stress Adaptation and ProgressionRC1CA147961 · NCI · RUTGERS, THE STATE UNIV OF N.J. · PI COLLER, HILARY A, RABINOWITZ, JOSHUA D · 2009 to 2010
$1.0M
NCATS NIH HHS UL1 TR000124NCATS NIH HHS UL1 TR001881NCI NIH HHS RC1 CA147961NIAMS NIH HHS R01 AR070245NIGMS NIH HHS R01 GM081686NIGMS NIH HHS R01 GM086465
6 · The paper itself

Abstract

Cell migration is essential for proper development and the defense against pathogens. Our previous work detailed a pathway of REversion-inducing-Cysteine-rich protein with Kazal motifs (RECK) isoform-mediated invasion in which a shorter RECK protein competes with MMP9 for interaction with the canonical RECK protein on the cell surface. Here we demonstrate that the mechanism through which RECK isoforms affect cell migration is mediated through changes in the levels of post-translational modifications (PTM) of α-tubulin. We show that both the canonical and short RECK isoforms modulate levels of tubulin acetylation and detyrosination. We demonstrate that these changes are sufficient to modulate the rate of fibroblast migration. If these tubulin PTMs are not altered, the effects of the canonical RECK isoform on cell migration are reversed. In defining the molecular pathway linking RECK and tubulin PTMs, we found that MMP9 and integrin activity both act as upstream regulators of tubulin acetylation and detyrosination. Overall, we propose a mechanism in which RECK isoforms on the cell surface have opposing effects on cell migration through MMP9-modulated changes to integrin-extracellular matrix (ECM) interactions that, in turn, affect microtubule PTMs.

Indexed as

Protein Processing, Post-TranslationalCell MembraneCell MovementExtracellular MatrixFibroblastsGene Expression RegulationGPI-Linked ProteinsHumansMatrix Metalloproteinase 9MicrotubulesSignal TransductionTubulinTubulin ModulatorsGPI-Linked ProteinsMatrix Metalloproteinase 9MMP9 protein, humanRECK protein, humanTubulinTubulin ModulatorsFibroblast migrationIntegrinMMP9RECK isoformsTubulin PTM

Identifiers

PMID30704758
PMCPMC7217981
OpenAlexW2912680147

What OpenQuestion holds

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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.