Evidence map›Paper›PMID 18710924›Full record

ArticleThe Journal of cell biology2008

Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation.

Manojkumar Valiyaveettil, Amber A Bentley, Priya Gursahaney, Rajaa Hussien, Ritu Chakravarti, Nina Kureishy, Soren Prag, Josephine C Adams

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

42 citing papers in PubMed, 64 citations in OpenAlex.

  1. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
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  3. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
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  17. Pancreatic Cancer Genetics.International journal of biological sciences · 2016
    Review
  18. Article
  19. Article
  20. Article
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

8 authors at 2 institutions in 2 countries.

Manojkumar ValiyaveettilDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Amber A Bentley
Priya Gursahaney
Rajaa Hussien
Ritu Chakravarti
Nina Kureishy
Soren Prag
Josephine C Adams
Cleveland Clinic Lerner College of Medicine · USMRC Laboratory for Molecular Cell Biology · GB

Funding

Fascin Protrusions in ECM-Cytoskeletal NetworkingR01GM068073 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI ADAMS, JOSEPHINE C · 2003 to 2007
$1.5M
NIGMS NIH HHS GM068073NIGMS NIH HHS R01 GM068073Wellcome TrustWellcome Trust 038284
6 · The paper itself

Abstract

The evolutionarily conserved kelch-repeat protein muskelin was identified as an intracellular mediator of cell spreading. We discovered that its morphological activity is controlled by association with RanBP9/RanBPM, a protein involved in transmembrane signaling and a conserved intracellular protein complex. By subcellular fractionation, endogenous muskelin is present in both the nucleus and the cytosol. Muskelin subcellular localization is coregulated by its C terminus, which provides a cytoplasmic restraint and also controls the interaction of muskelin with RanBP9, and its atypical lissencephaly-1 homology motif, which has a nuclear localization activity which is regulated by the status of the C terminus. Transient or stable short interfering RNA-based knockdown of muskelin resulted in protrusive cell morphologies with enlarged cell perimeters. Morphology was specifically restored by complementary DNAs encoding forms of muskelin with full activity of the C terminus for cytoplasmic localization and RanBP9 binding. Knockdown of RanBP9 resulted in equivalent morphological alterations. These novel findings identify a role for muskelin-RanBP9 complex in pathways that integrate cell morphology regulation and nucleocytoplasmic communication.

Indexed as

Cell ShapeActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceAnimalsCell Adhesion MoleculesCell NucleusChlorocebus aethiopsCOS CellsCytoskeletal ProteinsExportin 1 ProteinHumansIntracellular Signaling Peptides and ProteinsKaryopherinsMiceAdaptor Proteins, Signal TransducingCell Adhesion MoleculesCytoskeletal ProteinsExportin 1 ProteinIntracellular Signaling Peptides and ProteinsKaryopherinsMKLN1 protein, humanMkln1 protein, mouseNuclear Localization SignalsNuclear ProteinsRan binding protein 9Receptors, Cytoplasmic and Nuclear

Identifiers

PMID18710924
PMCPMC2518711
OpenAlexW2024718473

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.