Evidence map›Paper›PMID 35293963›Full record

ArticleThe Journal of cell biology2022

Ubiquitylation by Rab40b/Cul5 regulates Rap2 localization and activity during cell migration.

Emily D Duncan, Ke-Jun Han, Margaret A Trout, Rytis Prekeris

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  5. Proteasome stress activates YAP/TAZ through the RAP2-MAP4Ks-LATS1/2 pathway and its therapeutic implications in solid tumors.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Emily D DuncanDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO.ORCID 0000-0003-2062-2942
Ke-Jun HanDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO.
Margaret A TroutDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO.
Rytis PrekerisDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO.ORCID 0000-0003-3393-1963
University of Colorado Anschutz Medical Campus · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
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
NCI NIH HHS P30 CA046934NIGMS NIH HHS R01 GM122768NIGMS NIH HHS T32 GM008730NIGMS NIH HHS T32 GM136444NIH HHS NIH-T32-GM008730
6 · The paper itself

Abstract

Cell migration is a complex process that involves coordinated changes in membrane transport and actin cytoskeleton dynamics. Ras-like small monomeric GTPases, such as Rap2, play a key role in regulating actin cytoskeleton dynamics and cell adhesions. However, how Rap2 function, localization, and activation are regulated during cell migration is not fully understood. We previously identified the small GTPase Rab40b as a regulator of breast cancer cell migration. Rab40b contains a suppressor of cytokine signaling (SOCS) box, which facilitates binding to Cullin5, a known E3 ubiquitin ligase component responsible for protein ubiquitylation. In this study, we show that the Rab40b/Cullin5 complex ubiquitylates Rap2. Importantly, we demonstrate that ubiquitylation regulates Rap2 activation as well as recycling of Rap2 from the endolysosomal compartment to the lamellipodia of migrating breast cancer cells. Based on these data, we propose that Rab40b/Cullin5 ubiquitylates and regulates Rap2-dependent actin dynamics at the leading edge, a process that is required for breast cancer cell migration and invasion.

Indexed as

Breast NeoplasmsCullin Proteinsrap GTP-Binding ProteinsActin CytoskeletonCell MovementFemaleHumansPseudopodiaTranscription FactorsUbiquitinationUbiquitin-Protein LigasesCUL5 protein, humanCullin ProteinsRAP2A protein, humanrap GTP-Binding ProteinsTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID35293963
PMCPMC8931537
OpenAlexW4225808817

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.