Evidence map›Paper›PMID 25947155›Full record

ArticleBMC cell biology2015

Regulation of the microtubular cytoskeleton by Polycystin-1 favors focal adhesions turnover to modulate cell adhesion and migration.

Maddalena Castelli, Chiara De Pascalis, Gianfranco Distefano, Nadia Ducano, Amanda Oldani, Letizia Lanzetti, Alessandra Boletta

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Intestinal barrier function declines during polycystic kidney disease progression.American journal of physiology. Renal physiology · 2025
    Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Integrin-βAmerican journal of physiology. Renal physiology · 2020
    Article
  18. Article
  19. Article
  20. Polycystic kidney disease.Nature reviews. Disease primers · 2018
    Review
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

7 authors at 2 institutions in 1 country.

Maddalena CastelliDivision of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy. castelli.maddalena@hsr.it.
Chiara De PascalisDivision of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy. chiara.de-pascalis@pasteur.fr.
Gianfranco DistefanoDivision of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy. distefano.gianfranco@hsr.it.
Nadia DucanoCandiolo Cancer Institute, Candiolo, Torino, Italy. nadia.ducano@ircc.it.
Amanda OldaniIFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy. amanda.oldani@ifom.eu.
Letizia LanzettiCandiolo Cancer Institute, Candiolo, Torino, Italy. letizia.lanzetti@ircc.it.
Alessandra BolettaDivision of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy. boletta.alessandra@hsr.it.
Candiolo Cancer Institute · ITFIRC Institute of Molecular Oncology · IT

Funding

Telethon GGP12183
6 · The paper itself

Abstract

backgroundPolycystin-1 (PC-1) is a large plasma membrane receptor, encoded by the PKD1 gene, which is mutated in most cases of Autosomal Dominant Polycystic Kidney Disease (ADPKD). The disease is characterized by renal cysts. The precise function of PC-1 remains elusive, although several studies suggest that it can regulate the cellular shape in response to external stimuli. We and others reported that PC-1 regulates the actin cytoskeleton and cell migration.

resultsHere we show that cells over-expressing PC-1 display enhanced adhesion rates to the substrate, while cells lacking PC-1 have a reduced capability to adhere. In search for the mechanism responsible for this new property of PC-1 we found that this receptor is able to regulate the stability of the microtubules, in addition to its capability to regulate the actin cytoskeleton. The two cytoskeletal components are acting in a coordinated fashion. Notably, we uncovered that PC-1 regulation of the microtubule cytoskeleton impacts on the turnover rates of focal adhesions in migrating cells and we link all these properties to the capability of PC-1 to regulate the activation state of Focal Adhesion Kinase (FAK).

conclusionsIn this study we show several new features of the PC-1 receptor in modulating microtubules and adhesion dynamics, which are essential for its capability to regulate migration.

Indexed as

Actin CytoskeletonAnimalsCell AdhesionCell LineCell MovementDogsFluorescence Recovery After PhotobleachingFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsMadin Darby Canine Kidney CellsMiceMicrotubulesRNA InterferenceRNA, Small InterferingTRPP Cation ChannelsFocal Adhesion Protein-Tyrosine KinasesRNA, Small InterferingTRPP Cation Channels

Identifiers

PMID25947155
PMCPMC4437554
OpenAlexW2142827110

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.