Evidence map›Paper›PMID 10562284›Full record

ArticleThe Journal of cell biology1999

A role for p21-activated kinase in endothelial cell migration.

W B Kiosses, R H Daniels, C Otey, G M Bokoch, M A Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

103 citing papers in PubMed, 295 citations in OpenAlex.

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  5. Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
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43 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

W B KiossesDepartment of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
R H Daniels
C Otey
G M Bokoch
M A Schwartz
Scripps Research Institute · USUniversity of North Carolina at Chapel Hill · US

Funding

The Rho Family GTPases in Integrin SignalingR01GM047214 · NIGMS · YALE UNIVERSITY · PI SCHWARTZ, MARTIN A · 1991 to 2020
$6.3M
REGULATION OF NEUTROPHIL RECEPTOR/G PROTEIN INTERACTIONSR01GM039434 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BOKOCH, GARY M · 1988 to 2009
$4.7M
NHLBI NIH HHS HL44428NIGMS NIH HHS GM39434NIGMS NIH HHS GM47214NIGMS NIH HHS R01 GM039434NIGMS NIH HHS R01 GM047214
6 · The paper itself

Abstract

The serine/threonine p21-activated kinase (PAK) is an effector for Rac and Cdc42, but its role in regulating cytoskeletal organization has been controversial. To address this issue, we investigated the role of PAK in migration of microvascular endothelial cells. We found that a dominant negative (DN) mutant of PAK significantly inhibited cell migration and increased stress fibers and focal adhesions. The DN effect mapped to the most NH(2)-terminal proline-rich SH3-binding sequence. Observation of a green fluorescent protein-tagged alpha-actinin construct in living cells revealed that the DN construct had no effect on membrane ruffling, but dramatically inhibited stress fiber and focal contact motility and turnover. Constitutively active PAK inhibited migration equally well and also increased stress fibers and focal adhesions, but had a somewhat weaker effect on their dynamics. In contrast to their similar effects on motility, DN PAK decreased cell contractility, whereas active PAK increased contractility. Active PAK also increased myosin light chain (MLC) phosphorylation, as indicated by staining with an antibody to phosphorylated MLC, whereas DN PAK had little effect, despite the increase in actin stress fibers. These results demonstrate that although PAK is not required for extension of lamellipodia, it has substantial effects on cell adhesion and contraction. These data suggest a model in which PAK plays a role coordinating the formation of new adhesions at the leading edge with contraction and detachment at the trailing edge.

Indexed as

ActininAnimalsCell AdhesionCell LineCell MovementCOS CellsEndothelium, VascularGreen Fluorescent ProteinsLuminescent ProteinsMicrocirculationMicroscopy, VideoModels, BiologicalMyosin Light Chainsp21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesActininGreen Fluorescent ProteinsLuminescent ProteinsMyosin Light Chainsp21-Activated KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRecombinant ProteinsVinculin

Identifiers

PMID10562284
PMCPMC2156168
OpenAlexW2144240811

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.