Evidence map›Paper›PMID 33999101›Full record

ArticleThe Journal of cell biology2021

Rab40-Cullin5 complex regulates EPLIN and actin cytoskeleton dynamics during cell migration.

Erik S Linklater, Emily D Duncan, Ke-Jun Han, Algirdas Kaupinis, Mindaugas Valius, Traci R Lyons, Rytis Prekeris

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Erik S LinklaterDepartment of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO.
Emily D DuncanDepartment of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO.ORCID 0000-0003-2062-2942
Ke-Jun HanDepartment of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO.
Algirdas KaupinisProteomics Center, Institute of Biochemistry, Vilnius University Life Sciences Center, Vilnius, Lithuania.
Mindaugas ValiusProteomics Center, Institute of Biochemistry, Vilnius University Life Sciences Center, Vilnius, Lithuania.ORCID 0000-0001-8478-8517
Traci R LyonsDivision of Medical Oncology, Department of Medicine, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO.ORCID 0000-0002-8876-0391
Rytis PrekerisDepartment of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO.ORCID 0000-0003-3393-1963
University of Colorado Anschutz Medical Campus · USVilnius University · LTUniversity of Colorado Cancer Center · US

Funding

Predoctoral Training Program in Molecular and Cellular Biology (Supplement: Mentoring in the Research Environment)T32GM136444 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MICHAEL A MCMURRAY, Rytis Prekeris · 2020 to 2026
$3.7M
Predoctoral Training Program in Molecular BiologyT32GM008730 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI PREKERIS, RYTIS, SCLAFANI, ROBERT A · 1999 to 2019
$3.3M
The mechanisms regulating actin dynamics and polarized membrane transport during invadopodia formationR01GM122768 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI PREKERIS, RYTIS · 2018 to 2025
$2.6M
NIGMS NIH HHS R01 GM122768NIGMS NIH HHS T32 GM008730NIGMS NIH HHS T32 GM136444
6 · The paper itself

Abstract

Rab40b is a SOCS box-containing protein that regulates the secretion of MMPs to facilitate extracellular matrix remodeling during cell migration. Here, we show that Rab40b interacts with Cullin5 via the Rab40b SOCS domain. We demonstrate that loss of Rab40b-Cullin5 binding decreases cell motility and invasive potential and show that defective cell migration and invasion stem from alteration to the actin cytoskeleton, leading to decreased invadopodia formation, decreased actin dynamics at the leading edge, and an increase in stress fibers. We also show that these stress fibers anchor at less dynamic, more stable focal adhesions. Mechanistically, changes in the cytoskeleton and focal adhesion dynamics are mediated in part by EPLIN, which we demonstrate to be a binding partner of Rab40b and a target for Rab40b-Cullin5-dependent localized ubiquitylation and degradation. Thus, we propose a model where Rab40b-Cullin5-dependent ubiquitylation regulates EPLIN localization to promote cell migration and invasion by altering focal adhesion and cytoskeletal dynamics.

Indexed as

Actin CytoskeletonActinsCell MovementCytoskeletal ProteinsExtracellular MatrixFocal AdhesionsHumansStress FibersActinsCytoskeletal ProteinsLIMA1 protein, human

Identifiers

PMID33999101
PMCPMC8129794
OpenAlexW3162819630

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.