Evidence map›Paper›PMID 9802902›Full record

ArticleMolecular biology of the cell1998

Remodeling of the actin cytoskeleton is coordinately regulated by protein kinase C and the ADP-ribosylation factor nucleotide exchange factor ARNO.

S R Frank, J C Hatfield, J E Casanova

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 128 citations in OpenAlex.

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  4. Computer simulations of protein-membrane systems.Progress in molecular biology and translational science · 2020
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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 2 institutions in 2 countries.

S R FrankCombined Program in Pediatric Gastroenterology and Nutrition, Massachusetts General Hospital East, Charlestown, Massachusetts 02129, USA.
J C Hatfield
J E Casanova
Massachusetts General Hospital · USHarvard University · US

Funding

Xenograft and Isograft CoreP01DK033506 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI MCCORMICK, BETH A · 1986 to 2015
$24.2M
SIGNALLING IN MESANGIAL CELLS--CALCIUM AND PHOPHOLIPASESP01DK038452 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS · 1987 to 2012
$20.1M
TRANSEPITHELIAL TRANSPORT OF IMMUNOGLOBULINSR01AI032991 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI CASANOVA, JAMES E. · 1998 to 2002
$713k
TRANSPORT OF IMMUNOGLOBULINS ACROSS EPITHELIAR29AI032991 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI CASANOVA, JAMES E. · 1993 to 1997
–
NIAID NIH HHS AI-32991NIDDK NIH HHS DK-33506NIDDK NIH HHS DK-38452NIDDK NIH HHS P01 DK033506NIDDK NIH HHS P01 DK038452
6 · The paper itself

Abstract

ARNO is a member of a family of guanine-nucleotide exchange factors with specificity for the ADP-ribosylation factor (ARF) GTPases. ARNO possesses a central catalytic domain with homology to yeast Sec7p and an adjacent C-terminal pleckstrin homology (PH) domain. We have previously shown that ARNO localizes to the plasma membrane in vivo and efficiently catalyzes ARF6 nucleotide exchange in vitro. In addition to a role in endocytosis, ARF6 has also been shown to regulate assembly of the actin cytoskeleton. To determine whether ARNO is an upstream regulator of ARF6 in vivo, we examined the distribution of actin in HeLa cells overexpressing ARNO. We found that, while expression of ARNO leads to disassembly of actin stress fibers, it does not result in obvious changes in cell morphology. However, treatment of ARNO transfectants with the PKC agonist phorbol 12-myristate 13-acetate results in the dramatic redistribution of ARNO, ARF6, and actin into membrane protrusions resembling lamellipodia. This process requires ARF activation, as actin rearrangement does not occur in cells expressing a catalytically inactive ARNO mutant. PKC phosphorylates ARNO at a site immediately C-terminal to its PH domain. However, mutation of this site had no effect on the ability of ARNO to regulate actin rearrangement, suggesting that phosphorylation of ARNO by PKC does not positively regulate its activity. Finally, we demonstrate that an ARNO mutant lacking the C-terminal PH domain no longer mediates cytoskeletal reorganization, indicating a role for this domain in appropriate membrane localization. Taken together, these data suggest that ARNO represents an important link between cell surface receptors, ARF6, and the actin cytoskeleton.

Indexed as

GTPase-Activating ProteinsActinsAdenosine Diphosphate RiboseADP-Ribosylation FactorsAndrostadienesBrefeldin ACatalysisCytoskeletonEnzyme InhibitorsGene ExpressionGTP-Binding ProteinsHeLa CellsHumansProtein Kinase CProtein Synthesis InhibitorsWortmanninActinsAdenosine Diphosphate RiboseADP-Ribosylation FactorsAndrostadienesBrefeldin Acytohesin-2Enzyme InhibitorsGTPase-Activating ProteinsGTP-Binding ProteinsProtein Kinase CProtein Synthesis InhibitorsWortmannin

Identifiers

PMID9802902
PMCPMC25600
OpenAlexW2145402242

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.