Evidence map›Paper›PMID 20473878›Full record

ArticleInternational journal of cancer2011

Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells.

Meghna U Naik, Ngoc T Pham, Kristin Beebe, Wei Dai, Ulhas P Naik

Abstract read
In one paragraph

Article in International journal of cancer, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Miro proteins and their role in mitochondrial transfer in cancer and beyond.Frontiers in cell and developmental biology · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. CIB1: a small protein with big ambitions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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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 3 institutions in 1 country.

Meghna U NaikDelaware Cardiovascular Research Center, University of Delaware, Newark, DE 19716, USA. unaik@udel.edu
Ngoc T Pham
Kristin Beebe
Wei Dai
Ulhas P Naik
University of Delaware · USBiotechnology Institute · USNew York University · US

Funding

TOWARDS SOLID-STATE NMR STRUCTURES OF GPCRSP20RR015588 · NCRR · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2000 to 2009
$18.2M
Modulation of integrin function by cytoplasmic signalsR01HL057630 · NHLBI · UNIVERSITY OF DELAWARE · PI NAIK, ULHAS P · 2004 to 2007
$1.3M
MODULATION OF INTEGRIN FUNCTION BY CYTOPLASMIC SIGNALINGR29HL057630 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI NAIK, ULHAS P · 1997 to 2001
$222k
NCRR NIH HHS 1P20RR155801NCRR NIH HHS P20 RR015588NHLBI NIH HHS HL57630NHLBI NIH HHS R01 HL057630NHLBI NIH HHS R29 HL057630
6 · The paper itself

Abstract

Members of the polo-like kinases (Plk1, Plk2, Plk3 and Plk4) are involved in the regulation of various stages of the cell cycle and have been implicated in cancer progression. Unlike its other family members, the expression of Plk3 remains steady during cell cycle progression, suggesting that its activity may be spatiotemporally regulated. However, the mechanism of regulation of Plk3 activity is not well understood. Here, we show that calcium- and integrin-binding protein 1 (CIB1), a Plk3 interacting protein, is widely expressed in various cancer cell lines. Expression of CIB1 mRNA as well as protein is increased in breast cancer tissue as compared to normal tissue. CIB1 constitutively interacts with Plk3 as determined by both in vitro and in vivo assays. This interaction of CIB1 with Plk3 is independent of intracellular Ca(2+). Furthermore, binding of CIB1 results in inhibition of Plk3 kinase activity both in vitro and in vivo. Interestingly, this inhibition of the Plk3 activity by CIB1 is Ca(2+)-dependent. Taken together, our results suggest that CIB1 is a regulatory subunit of Plk3 and it regulates Plk3 activity in a Ca(2+)-dependent manner. Furthermore, upregulation of CIB1 in cancer cells could thus inhibit Plk3 activity leading to abnormal cell cycle regulation in breast cancer cells. Thus, in addition to Plk3, CIB1 may be a potential biomarker and target for therapeutic intervention of breast cancer.

Indexed as

Base SequenceBreast NeoplasmsCalciumCalcium-Binding ProteinsCell Line, TumorFemaleHumansImmunohistochemistryPolo-like KinasesProtein BindingProtein Serine-Threonine KinasesRecombinant ProteinsRNA, Double-StrandedRNA InterferenceRNA, MessengerRNA, Small InterferingCalciumCalcium-Binding ProteinsCIB1 protein, humanPLK3 protein, humanPolo-like KinasesProtein Serine-Threonine KinasesRecombinant ProteinsRNA, Double-StrandedRNA, MessengerRNA, Small InterferingTumor Suppressor Proteins

Identifiers

PMID20473878
PMCPMC2954264
OpenAlexW2001985328

What OpenQuestion holds

Textmetadata
LicenceTDM
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.