Evidence map›Paper›PMID 31806702›Full record

ArticleThe Journal of biological chemistry2020

DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA.

Rakesh Joshi, Lyugao Qin, Xuan Cao, Shanshan Zhong, Courtney Voss, Weiping Min, Shawn S C Li

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-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

19 citing papers in PubMed, 35 citations in OpenAlex.

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  9. Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
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  17. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
    Review
  18. Article
  19. 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

7 authors at 2 institutions in 2 countries.

Rakesh JoshiDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada; Departments of Surgery, Pathology and Oncology, Western University, London, Ontario N6A 5A5, Canada.
Lyugao QinDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada.
Xuan CaoSchool of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
Shanshan ZhongDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada.
Courtney VossDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada.
Weiping MinDepartments of Surgery, Pathology and Oncology, Western University, London, Ontario N6A 5A5, Canada. Electronic address: weiping.min@uwo.ca.
Shawn S C LiDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada. Electronic address: sli@uwo.ca.
Western University · CAHuazhong University of Science and Technology · CN

Funding

CIHR
6 · The paper itself

Abstract

Deleted-in-liver cancer 1 (DLC1) exerts its tumor suppressive function mainly through the Rho-GTPase-activating protein (RhoGAP) domain. When activated, the domain promotes the hydrolysis of RhoA-GTP, leading to reduced cell migration. DLC1 is kept in an inactive state by an intramolecular interaction between its RhoGAP domain and the DLC1 sterile α motif (SAM) domain. We have shown previously that this autoinhibited state of DLC1 may be alleviated by tensin-3 (TNS3) or PTEN. We show here that the TNS3/PTEN-DLC1 interactions are mediated by the C2 domains of the former and the SAM domain of the latter. Intriguingly, the DLC1 SAM domain was capable of binding to specific peptide motifs within the C2 domains. Indeed, peptides containing the binding motifs were highly effective in blocking the C2-SAM domain-domain interaction. Importantly, when fused to the

Indexed as

Cell ProliferationBreast NeoplasmsCell Line, TumorCell MovementFemaleGTPase-Activating ProteinsHEK293 CellsHumansModels, MolecularPeptide FragmentsProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsPTEN PhosphohydrolaserhoA GTP-Binding ProteinSterile Alpha MotifDLC1 protein, humanGTPase-Activating ProteinsPeptide FragmentsPTEN PhosphohydrolasePTEN protein, humanrhoA GTP-Binding ProteinRHOA protein, humanTensinsTNS3 protein, humanTumor Suppressor Proteinsbreast cancerC2 domaincell migrationcell proliferationdeleted in liver cancer 1 (DLC1)Ras homolog gene family, member A (RhoA)RhoGAPSAM domain

Identifiers

PMID31806702
PMCPMC6956525
OpenAlexW2992552168

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.