Evidence map›Paper›PMID 31601460›Full record

ArticleStructure (London, England : 1993)2019

Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes.

Sanchaita Das, Andrew W Malaby, Agata Nawrotek, Wenhua Zhang, Mahel Zeghouf, Sarah Maslen, Mark Skehel, Srinivas Chakravarthy, Thomas C Irving, Osman Bilsel and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 3 countries.

Sanchaita DasProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Andrew W MalabyProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Agata NawrotekCNRS and Ecole Normale Supérieure Paris-Saclay, 94235 Cachan, France.
Wenhua ZhangCNRS and Ecole Normale Supérieure Paris-Saclay, 94235 Cachan, France.
Mahel ZeghoufCNRS and Ecole Normale Supérieure Paris-Saclay, 94235 Cachan, France.
Sarah MaslenMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Mark SkehelMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Srinivas ChakravarthyThe Biophysics Collaborative Access Team (BioCAT), Department of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA.
Thomas C IrvingThe Biophysics Collaborative Access Team (BioCAT), Department of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA.
Osman BilselDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Jacqueline CherfilsCNRS and Ecole Normale Supérieure Paris-Saclay, 94235 Cachan, France. Electronic address: jacqueline.cherfils@ens-paris-saclay.fr.
David G LambrightProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01655, USA. Electronic address: david.lambright@umassmed.edu.
University of Massachusetts Chan Medical School · USCentre National de la Recherche Scientifique · FRIllinois Institute of Technology · USMRC Laboratory of Molecular Biology · GBÉcole Normale Supérieure Paris-Saclay · FR

Funding

Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
STRUCTURAL BASIS OF G PROTEIN MEDIATED SIGNALINGR01GM056324 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LAMBRIGHT, DAVID G · 1998 to 2018
$6.2M
Medical Research Council MC_U105184326NIGMS NIH HHS P41 GM103622NIGMS NIH HHS R01 GM056324
6 · The paper itself

Abstract

Membrane dynamic processes require Arf GTPase activation by guanine nucleotide exchange factors (GEFs) with a Sec7 domain. Cytohesin family Arf GEFs function in signaling and cell migration through Arf GTPase activation on the plasma membrane and endosomes. In this study, the structural organization of two cytohesins (Grp1 and ARNO) was investigated in solution by size exclusion-small angle X-ray scattering and negative stain-electron microscopy and on membranes by dynamic light scattering, hydrogen-deuterium exchange-mass spectrometry and guanosine diphosphate (GDP)/guanosine triphosphate (GTP) exchange assays. The results suggest that cytohesins form elongated dimers with a central coiled coil and membrane-binding pleckstrin-homology (PH) domains at opposite ends. The dimers display significant conformational heterogeneity, with a preference for compact to intermediate conformations. Phosphoinositide-dependent membrane recruitment is mediated by one PH domain at a time and alters the conformational dynamics to prime allosteric activation by Arf-GTP. A structural model for membrane targeting and allosteric activation of full-length cytohesin dimers is discussed.

Indexed as

Amino Acid MotifsAnimalsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsGTPase-Activating ProteinsGuanosine DiphosphateGuanosine TriphosphateKineticsLiposomesMiceModels, MolecularPhosphatidylinositol 4,5-Diphosphatecytohesin-2GTPase-Activating ProteinsGuanosine DiphosphateGuanosine TriphosphateLiposomesPhosphatidylinositol 4,5-Diphosphatephosphatidylinositol receptorsReceptors, Cytoplasmic and NuclearRecombinant ProteinsautoinhibitionDLSEMGEFHDXMSNSSAXSSECstructure

Identifiers

PMID31601460
PMCPMC6948192
OpenAlexW2977852089

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.