Evidence map›Paper›PMID 26620550›Full record

ArticleThe EMBO journal2016

PTPRN2 and PLCβ1 promote metastatic breast cancer cell migration through PI(4,5)P2-dependent actin remodeling.

Caitlin A Sengelaub, Kristina Navrazhina, Jason B Ross, Nils Halberg, Sohail F Tavazoie

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
2.7field-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

81 citing papers in PubMed, 116 citations in OpenAlex.

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21 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Caitlin A SengelaubLaboratory of Systems Cancer Biology, Rockefeller University, New York, NY, USA.
Kristina NavrazhinaLaboratory of Systems Cancer Biology, Rockefeller University, New York, NY, USA.
Jason B RossLaboratory of Systems Cancer Biology, Rockefeller University, New York, NY, USA.
Nils HalbergLaboratory of Systems Cancer Biology, Rockefeller University, New York, NY, USA.
Sohail F TavazoieLaboratory of Systems Cancer Biology, Rockefeller University, New York, NY, USA stavazoie@rockefeller.edu.
Rockefeller University · US

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
NIGMS NIH HHS GM007739NIGMS NIH HHS T32 GM007739NIGMS NIH HHS T32GM007739
6 · The paper itself

Abstract

Altered abundance of phosphatidyl inositides (PIs) is a feature of cancer. Various PIs mark the identity of diverse membranes in normal and malignant cells. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) resides predominantly in the plasma membrane, where it regulates cellular processes by recruiting, activating, or inhibiting proteins at the plasma membrane. We find that PTPRN2 and PLCβ1 enzymatically reduce plasma membrane PI(4,5)P2 levels in metastatic breast cancer cells through two independent mechanisms. These genes are upregulated in highly metastatic breast cancer cells, and their increased expression associates with human metastatic relapse. Reduction in plasma membrane PI(4,5)P2 abundance by these enzymes releases the PI(4,5)P2-binding protein cofilin from its inactive membrane-associated state into the cytoplasm where it mediates actin turnover dynamics, thereby enhancing cellular migration and metastatic capacity. Our findings reveal an enzymatic network that regulates metastatic cell migration through lipid-dependent sequestration of an actin-remodeling factor.

Indexed as

Cell MovementActin Depolymerizing FactorsActinsAnimalsBreast NeoplasmsCell Line, TumorHumansMice, SCIDPhosphatidylinositol 4,5-DiphosphatePhospholipase C betaReceptor-Like Protein Tyrosine Phosphatases, Class 8Actin Depolymerizing FactorsActinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C betaPLCB1 protein, humanPTPRN2 protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 8actinmetastasisphosphoinositidesPI(4,5)P2tumor migration

Identifiers

PMID26620550
PMCPMC4717998
OpenAlexW2188455587

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.