Evidence map›Paper›PMID 25561548›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Single-molecule tracking of small GTPase Rac1 uncovers spatial regulation of membrane translocation and mechanism for polarized signaling.

Sulagna Das, Taofei Yin, Qingfen Yang, Jingqiao Zhang, Yi I Wu, Ji Yu

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

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  7. Redox Regulation of Cell Migration via Nischarin S-glutathionylation.bioRxiv : the preprint server for biology · 2025
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  9. Emerging oralFrontiers in oral health · 2025
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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

6 authors at 1 institution in 1 country.

Sulagna DasCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030.
Taofei YinCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030.
Qingfen YangCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030.
Jingqiao ZhangCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030.
Yi I WuCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030.
Ji YuCenter for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030 jyu@uchc.edu.
UConn Health · US

Funding

Bacterial cytoskeletal structures and dynamics at single molecule levelR01GM085301 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI YU, JI · 2009 to 2013
$1.4M
Engineering a new class of optogenetic tools targeting small GTPases and kinasesR21NS071216 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WU, YI · 2010 to 2011
$411k
NIGMS NIH HHS R01 GM085301NIGMS NIH HHS R01GM085301NINDS NIH HHS R21 NS071216NINDS NIH HHS R21NS071216
6 · The paper itself

Abstract

Polarized Rac1 signaling is a hallmark of many cellular functions, including cell adhesion, motility, and cell division. The two steps of Rac1 activation are its translocation to the plasma membrane and the exchange of nucleotide from GDP to GTP. It is, however, unclear whether these two processes are regulated independent of each other and what their respective roles are in polarization of Rac1 signaling. We designed a single-particle tracking (SPT) method to quantitatively analyze the kinetics of Rac1 membrane translocation in living cells. We found that the rate of Rac1 translocation was significantly elevated in protrusions during cell spreading on collagen. Furthermore, combining FRET sensor imaging with SPT measurements in the same cell, the recruitment of Rac1 was found to be polarized to an extent similar to that of the nucleotide exchange process. Statistical analysis of single-molecule trajectories and optogenetic manipulation of membrane lipids revealed that Rac1 membrane translocation precedes nucleotide exchange, and is governed primarily by interactions with phospholipids, particularly PI(3,4,5)P3, instead of protein factors. Overall, the study highlights the significance of membrane translocation in spatial Rac1 signaling, which is in addition to the traditional view focusing primarily on GEF distribution and exchange reaction.

Indexed as

Signal TransductionHumansKineticsMCF-7 CellsMicroscopy, FluorescenceProtein Transportrac1 GTP-Binding Proteinrac1 GTP-Binding Proteincell polarizationRac1RhoGTPasesptPALMsuper-resolution microscopy

Identifiers

PMID25561548
PMCPMC4311845
OpenAlexW2002939552

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.