Evidence map›Paper›PMID 24662836›Full record

ArticleOncogene2015

PDZ and LIM domain protein 1(PDLIM1)/CLP36 promotes breast cancer cell migration, invasion and metastasis through interaction with α-actinin.

Z Liu, Y Zhan, Y Tu, K Chen, Z Liu, C Wu

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Pooled it
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  18. Delta-Catenin as a Modulator of Rho GTPases in Neurons.Frontiers in cellular neuroscience · 2022
    Review
  19. Article
  20. The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022
    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

6 authors at 2 institutions in 2 countries.

Z LiuDepartment of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Y ZhanState Key Laboratory of Molecular Oncology, Cancer Institute and Hospital, Chinese Academy of Medical Sciences, Peking Union Medical College, Beijing, China.
Y TuDepartment of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
K ChenDepartment of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Z LiuState Key Laboratory of Molecular Oncology, Cancer Institute and Hospital, Chinese Academy of Medical Sciences, Peking Union Medical College, Beijing, China.
C Wu1] Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA [2] University of Pittsburgh Cancer Institute, Pittsburgh, PA, USA.
University of Pittsburgh · USChinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

PINCH-1 Interactions and FunctionsR01GM065188 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE · 2002 to 2014
$3.3M
NIGMS NIH HHS GM65188NIGMS NIH HHS R01 GM065188
6 · The paper itself

Abstract

Increased CLP36 expression has been found to be closely associated with breast cancer progression. However, whether and how it contributes to malignant behavior of breast cancer cells were not known. We show here that CLP36 is critical for promoting breast cancer cell migration and invasion in vitro and metastasis in vivo, whereas it is dispensable for breast cell proliferation and anchorage-independent growth in vitro and tumor growth in vivo. CLP36 interacted with both α-actinin-1 and -4 in breast cancer cells. Depletion of either α-actinin-1 or -4 inhibited breast cancer cell migration. Furthermore, mutations inhibiting the α-actinin-binding activity abolished the ability of CLP36 to promote breast cancer cell migration. Finally, depletion of CLP36 or disruption of the CLP36-α-actinin complex in breast cancer cells substantially inhibited Cdc42 activation, cell polarization and migration. Our results identify CLP36 as an important regulator of breast cancer cell migration and metastasis, and shed light on how increased CLP36 expression contributes to the progression of breast cancer.

Indexed as

ActininAnimalsBreast Neoplasmscdc42 GTP-Binding ProteinCell Line, TumorCell MovementCell ProliferationDisease Models, AnimalFemaleHeterograftsHumansLIM Domain ProteinsMiceNeoplasm InvasivenessNeoplasm MetastasisProtein BindingActinincdc42 GTP-Binding ProteinLDB2 protein, humanLIM Domain ProteinsTranscription Factors

Identifiers

PMID24662836
PMCPMC4175366
OpenAlexW2026241397

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.