Evidence map›Paper›PMID 15772154›Full record

ArticleMolecular biology of the cell2005

The unique N-terminus of R-ras is required for Rac activation and precise regulation of cell migration.

Stephen P Holly, Mark K Larson, Leslie V Parise

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

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  13. Integrin traffic - the update.Journal of cell science · 2015
    Review
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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.

Stephen P HollyDepartment of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Mark K Larson
Leslie V Parise
University of North Carolina at Chapel Hill · US

Funding

Integrated Training in Cancer Model SystemsT32CA009156 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DER, CHANNING J. · 1985 to 2020
$19.7M
THE ROLE OF THE VITAMIN K CYCLE IN COAGULATIONP01HL006350 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W · 1985 to 2013
$17.5M
THE ROLE OF RAP1 IN INTEGRIN ACTIVATION AND PLATELET SIGNALINGP01HL045100 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PARISE, LESLIE V. · 1993 to 2007
$13.7M
NCI NIH HHS CA09156NCI NIH HHS T32 CA009156NHLBI NIH HHS 2-P01-HL06350NHLBI NIH HHS 2-P01-HL45100NHLBI NIH HHS P01 HL006350NHLBI NIH HHS P01 HL045100
6 · The paper itself

Abstract

The Ras family GTPase, R-Ras, elicits important integrin-dependent cellular behaviors such as adhesion, spreading and migration. While oncogenic Ras GTPases and R-Ras share extensive sequence homology, R-Ras induces a distinct set of cellular behaviors. To explore the structural basis for these differences, we asked whether the unique N-terminal 26 amino acid extension of R-Ras was responsible for R-Ras-specific signaling events. Using a 32D mouse myeloid cell line, we show that full-length R-Ras activates Rac and induces Rac-dependent cell spreading. In contrast, truncated R-Ras lacking its first 26 amino acids fails to activate Rac, resulting in reduced cell spreading. Truncated R-Ras also stimulates more beta3 integrin-dependent cell migration than full-length R-Ras, suggesting that the N-terminus may negatively regulate cell movement. However, neither the subcellular localization of R-Ras nor its effects on cell adhesion are affected by the presence or absence of the N-terminus. These results indicate that the N-terminus of R-Ras positively regulates specific R-Ras functions such as Rac activation and cell spreading but negatively regulates R-Ras-mediated cell migration.

Indexed as

ActinsAmino Acid SequenceAnimalsBase SequenceCell AdhesionCell LineCell MembraneCell MovementDNAGTP PhosphohydrolasesMiceMolecular Sequence DataPhosphatidylinositol 3-KinasesPlatelet Glycoprotein GPIIb-IIIa Complexrac GTP-Binding Proteinsras ProteinsActinsDNAGTP PhosphohydrolasesPhosphatidylinositol 3-KinasesPlatelet Glycoprotein GPIIb-IIIa Complexrac GTP-Binding Proteinsras Proteinsrho GTP-Binding ProteinsRras protein, mouse

Identifiers

PMID15772154
PMCPMC1087249
OpenAlexW2118024265

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.