Evidence map›Paper›PMID 21209314›Full record

ArticleMolecular biology of the cell2011

A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration.

Susanne Ziegler, Tim Eiseler, Rolf-Peter Scholz, Alexander Beck, Gisela Link, Angelika Hausser

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
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  4. Protein kinase D signaling in cancer: A friend or foe?Biochimica et biophysica acta. Reviews on cancer · 2017
    Review
  5. Article
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  8. Review
  9. Protein kinase D2 silencing reduced motility of doxorubicin-resistant MCF7 cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
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  20. Overexpression of RIN1 associates with tumor grade and progression in patients of bladder urothelial carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2012
    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

6 authors at 1 institution in 1 country.

Susanne ZieglerInstitute of Cell Biology and Immunology, University of Stuttgart, 70569 Stuttgart, Germany Panatecs GmbH, 72070 Tübingen, Germany.
Tim Eiseler
Rolf-Peter Scholz
Alexander Beck
Gisela Link
Angelika Hausser
University of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multifunctional signal adapter protein Ras and Rab interactor 1 (RIN1) is a Ras effector protein involved in the regulation of epithelial cell processes such as cell migration and endocytosis. RIN1 signals via two downstream pathways, namely the activation of Rab5 and Abl family kinases. Protein kinase D (PKD) phosphorylates RIN1 at serine 351 in vitro, thereby regulating interaction with 14-3-3 proteins. Here, we report the identification of serine 292 in RIN1 as an in vivo PKD phosphorylation site. PKD-mediated phosphorylation at this site was confirmed with a phospho-specific antibody and by mass spectrometry. We demonstrate that phosphorylation at serine 292 controls RIN1-mediated inhibition of cell migration by modulating the activation of Abl kinases. We further provide evidence that RIN1 in vivo phosphorylation at serine 351 occurs independently of PKD. Collectively, our data identify a novel PKD signaling pathway through RIN1 and Abl kinases that is involved in the regulation of actin remodeling and cell migration.

Indexed as

Cell MovementActinsAmino Acid MotifsAmino Acid SequenceAntibodiesHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataPhosphorylationPhosphoserineProtein Kinase CProtein TransportProtein-Tyrosine KinasesSubcellular FractionsTumor Suppressor ProteinsActinsAntibodiesARG tyrosine kinaseIntracellular Signaling Peptides and ProteinsPhosphoserineProtein Kinase Cprotein kinase DProtein-Tyrosine KinasesRIN1 protein, humanTumor Suppressor Proteins

Identifiers

PMID21209314
PMCPMC3046055
OpenAlexW2090883234

What OpenQuestion holds

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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.