Evidence map›Paper›PMID 19812310›Full record

ArticleJournal of cell science2009

Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal morphogenesis via Rac signaling.

Marie-France Lisé, Deepak P Srivastava, Pamela Arstikaitis, Robyn L Lett, Razan Sheta, Vijay Viswanathan, Peter Penzes, Timothy P O'Connor, Alaa El-Husseini

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Rab10-CAV1 mediated intraluminal vesicle transport to migrasomes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  14. Article
  15. Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Functions of class V myosins in neurons.The Journal of biological chemistry · 2013
    Review
  20. Structural basis of cargo recognitions for class V myosins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

9 authors at 2 institutions in 2 countries.

Marie-France LiséDepartment of Psychiatry and Brain Research Center, University of British Columbia, Vancouver, BC, Canada. marief.lise@gmail.com
Deepak P Srivastava
Pamela Arstikaitis
Robyn L Lett
Razan Sheta
Vijay Viswanathan
Peter Penzes
Timothy P O'Connor
Alaa El-Husseini
University of British Columbia · CANorthwestern University · US

Funding

Small GTPase signaling in spinesR01MH071316 · NIMH · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BARBOLINA, MARIA V., PENZES, PETER · 2005 to 2025
$7.1M
NIMH NIH HHS MH 071316
6 · The paper itself

Abstract

Neuronal morphology plays an essential role in neuronal function. The establishment and maintenance of neuronal morphology is intimately linked to the actin cytoskeleton; however, the molecular mechanisms that regulate changes in neuronal morphology are poorly understood. Here we identify a novel myosin-Va (MyoVa)-interacting protein, RILPL2, which regulates cellular morphology. Overexpression of this protein in young or mature hippocampal neurons results in an increase in the number of spine-like protrusions. By contrast, knockdown of endogenous RILPL2 in neurons by short hairpin RNA (shRNA) interference results in reduced spine-like protrusions, a phenotype rescued by overexpression of an shRNA-insensitive RILPL2 mutant, suggesting a role for RILPL2 in both the establishment and maintenance of dendritic spines. Interestingly, we demonstrate that RILPL2 and the Rho GTPase Rac1 form a complex, and that RILPL2 is able to induce activation of Rac1 and its target, p21-activated kinase (Pak). Notably, both RILPL2-mediated morphological changes and activation of Rac1-Pak signaling were blocked by expression of a truncated tail form of MyoVa or MyoVa shRNA, demonstrating that MyoVa is crucial for proper RILPL2 function. This might represent a novel mechanism linking RILPL2, the motor protein MyoVa and Rac1 with neuronal structure and function.

Indexed as

Cell ShapeMorphogenesisAnimalsAxonsBrainCarrier ProteinsChlorocebus aethiopsCOS CellsDendritic SpinesEnzyme ActivationGene Expression RegulationGene Knockdown TechniquesGenes, DominantHippocampusMiceMyosin Heavy ChainsCarrier ProteinsMyo5a protein, ratMyosin Heavy ChainsMyosin Type Vrac GTP-Binding ProteinsRNA, Messenger

Identifiers

PMID19812310
PMCPMC2758809
OpenAlexW2044706782

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.