Evidence map›Paper›PMID 16966426›Full record

ArticleThe Journal of cell biology2006

RLIP76 (RalBP1) is an R-Ras effector that mediates adhesion-dependent Rac activation and cell migration.

Lawrence E Goldfinger, Celeste Ptak, Erin D Jeffery, Jeffrey Shabanowitz, Donald F Hunt, Mark H Ginsberg

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
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  3. Review
  4. Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer's Disease?International journal of molecular sciences · 2022
    Review
  5. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    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

6 authors at 4 institutions in 1 country.

Lawrence E GoldfingerDivision of Rheumatology, Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Celeste Ptak
Erin D Jeffery
Jeffrey Shabanowitz
Donald F Hunt
Mark H Ginsberg
Division of Chemistry · USCenter for Rheumatology · USUniversity of California, San Diego · USUniversity of Virginia · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
TYROSINE KINASE C-ABL AND BCR-ABL IN INTEGRIN DEPENDENT SIGNALINGP01HL057900 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHATTIL, SANFORD J · 1997 to 2012
$17.4M
NHLBI NIH HHS HL078784NHLBI NIH HHS HL57900NHLBI NIH HHS P01 HL057900NHLBI NIH HHS P01 HL078784NIGMS NIH HHS GM37537NIGMS NIH HHS R01 GM037537NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

The Ras family of small GTPases regulates cell proliferation, spreading, migration and apoptosis, and malignant transformation by binding to several protein effectors. One such GTPase, R-Ras, plays distinct roles in each of these processes, but to date, identified R-Ras effectors were shared with other Ras family members (e.g., H-Ras). We utilized a new database of Ras-interacting proteins to identify RLIP76 (RalBP1) as a novel R-Ras effector. RLIP76 binds directly to R-Ras in a GTP-dependent manner, but does not physically associate with the closely related paralogues H-Ras and Rap1A. RLIP76 is required for adhesion-induced Rac activation and the resulting cell spreading and migration, as well as for the ability of R-Ras to enhance these functions. RLIP76 regulates Rac activity through the adhesion-induced activation of Arf6 GTPase and activation of Arf6 bypasses the requirement for RLIP76 in Rac activation and cell spreading. Thus, we identify a novel R-Ras effector, RLIP76, which links R-Ras to adhesion-induced Rac activation through a GTPase cascade that mediates cell spreading and migration.

Indexed as

ADP-Ribosylation Factor 6ADP-Ribosylation FactorsAnimalsCell AdhesionCell MovementCell SizeFibroblastsGTPase-Activating ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMiceNIH 3T3 CellsProtein Bindingrac GTP-Binding Proteinsras ProteinsSignal TransductionADP-Ribosylation Factor 6ADP-Ribosylation FactorsArf6 protein, mouseGTPase-Activating ProteinsGTP PhosphohydrolasesGuanosine Triphosphaterac GTP-Binding ProteinsRalbp1 protein, mouseras ProteinsRras protein, mouse

Identifiers

PMID16966426
PMCPMC2064341
OpenAlexW2122437448

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.