Evidence map›Paper›PMID 16394104›Full record

ArticleMolecular biology of the cell2006

Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle.

Disha Dadke, Michael Jarnik, Elena N Pugacheva, Mahendra K Singh, Erica A Golemis

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.8field-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

37 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Review
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  8. Article
  9. Downregulation of Smurf2 ubiquitin ligase in pancreatic cancer cells reversed TGF-β-induced tumor formation.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  10. Review
  11. Issues in interpreting the in vivo activity of Aurora-A.Expert opinion on therapeutic targets · 2015
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Aurora A kinase (AURKA) in normal and pathological cell division.Cellular and molecular life sciences : CMLS · 2013
    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

5 authors at 1 institution in 2 countries.

Disha DadkeDivision of Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Michael Jarnik
Elena N Pugacheva
Mahendra K Singh
Erica A Golemis
Fox Chase Cancer Center · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
ROLES OF HEF1 IN CELL DIFFERENTIATION AND SURVIVALR01CA063366 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI GOLEMIS, ERICA A. · 1998 to 2013
$3.9M
CONTROL OF NORMAL AND ABNORMAL CELL GROWTHR29CA063366 · NCI · INSTITUTE FOR CANCER RESEARCH · PI GOLEMIS, ERICA A · 1994 to 1997
–
NCI NIH HHS CA06927NCI NIH HHS CA63366NCI NIH HHS P30 CA006927NCI NIH HHS R01 CA063366
6 · The paper itself

Abstract

The focal adhesion-associated signaling protein HEF1 undergoes a striking relocalization to the spindle at mitosis, but a function for HEF1 in mitotic signaling has not been demonstrated. We here report that overexpression of HEF1 leads to failure of cells to progress through cytokinesis, whereas depletion of HEF1 by small interfering RNA (siRNA) leads to defects earlier in M phase before cleavage furrow formation. These defects can be explained mechanistically by our determination that HEF1 regulates the activation cycle of RhoA. Inactivation of RhoA has long been known to be required for cytokinesis, whereas it has recently been determined that activation of RhoA at the entry to M phase is required for cellular rounding. We find that increased HEF1 sustains RhoA activation, whereas depleted HEF1 by siRNA reduces RhoA activation. Furthermore, we demonstrate that chemical inhibition of RhoA is sufficient to reverse HEF1-dependent cellular arrest at cytokinesis. Finally, we demonstrate that HEF1 associates with the RhoA-GTP exchange factor ECT2, an orthologue of the Drosophila cytokinetic regulator Pebble, providing a direct means for HEF1 control of RhoA. We conclude that HEF1 is a novel component of the cell division control machinery and that HEF1 activity impacts division as well as cell attachment signaling events.

Indexed as

Gene Expression RegulationAdaptor Proteins, Signal TransducingCytokinesisHumansMitosisModels, BiologicalPhosphoproteinsProtein TransportProto-Oncogene ProteinsrhoA GTP-Binding ProteinRNA, Small InterferingTumor Cells, CulturedAdaptor Proteins, Signal TransducingECT2 protein, humanNEDD9 protein, humanPhosphoproteinsProto-Oncogene ProteinsrhoA GTP-Binding ProteinRNA, Small Interfering

Identifiers

PMID16394104
PMCPMC1382310
OpenAlexW2106131396

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.