ArticleThe Journal of biological chemistry2008
Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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.
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.
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Who cites it
39 citing papers in PubMed, 71 citations in OpenAlex.
- Tensins in Cancer: Integration of Their Domain Functions, Context-Dependent Regulation and Biomarker Potential.Biology · 2025Review
- The circDUSP1/miR-429/DLC1 regulatory network affects proliferation, migration, and invasion of triple-negative breast cancer cells.Scientific reports · 2025Article
- Article
- Identification and characterization of intermediate states in mammalian neural crest cell epithelial to mesenchymal transition and delamination.bioRxiv : the preprint server for biology · 2024Article
- SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP.Nature communications · 2022Article
- Functional antagonism between CagA and DLC1 in gastric cancer.Cell death discovery · 2022Article
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Frequent Downregulation and Promoter Hypermethylation of DLC1: Relationship with Clinical Outcome in Gallbladder Cancer.Journal of gastrointestinal cancer · 2022Article
- Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022Review
- Identifying interactive biological pathways associated with reading disability.Brain and behavior · 2020Article
- Breakpoint Mapping of Symptomatic Balanced Translocations Links theJournal of clinical medicine · 2020Article
- DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA.The Journal of biological chemistry · 2020Article
- Intramitochondrial Src kinase links mitochondrial dysfunctions and aggressiveness of breast cancer cells.Cell death & disease · 2019Article
- SRC and ERK cooperatively phosphorylate DLC1 and attenuate its Rho-GAP and tumor suppressor functions.The Journal of cell biology · 2019Article
- Adhesions Assemble!-Autoinhibition as a Major Regulatory Mechanism of Integrin-Mediated Adhesion.Frontiers in molecular biosciences · 2019Review
- Whole exome sequencing identifies novel predisposing genes in neural tube defects.Molecular genetics & genomic medicine · 2019Article
- The extracellular matrix-myosin pathway in mechanotransduction: from molecule to tissue.Emerging topics in life sciences · 2018Article
- Effects of DLC1 Deficiency on Endothelial Cell Contact Growth Inhibition and Angiosarcoma Progression.Journal of the National Cancer Institute · 2018Article
- Functional analysis of the Drosophila RhoGAP Cv-c protein and its equivalence to the human DLC3 and DLC1 proteins.Scientific reports · 2018Article
- Asymmetric localization of DLC1 defines avian trunk neural crest polarity for directional delamination and migration.Nature communications · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
DLC-1 encodes a Rho GTPase-activating protein (RhoGAP) and negative regulator of specific Rho family proteins (RhoA-C and Cdc42). DLC-1 is a multi-domain protein, with the RhoGAP catalytic domain flanked by an amino-terminal sterile alpha motif (SAM) and a carboxyl-terminal START domain. The roles of these domains in the regulation of DLC-1 function remain to be determined. We undertook a structure-function analysis involving truncation and missense mutants of DLC-1. We determined that the amino-terminal SAM domain functions as an autoinhibitory domain of intrinsic RhoGAP activity. Additionally, we determined that the SAM and START domains are dispensable for DLC-1 association with focal adhesions. We then characterized several mutants for their ability to regulate cell migration and identified constitutively activated and dominant negative mutants of DLC-1. We report that DLC-1 activation profoundly alters cell morphology, enhances protrusive activity, and can increase the velocity but reduce directionality of cell migration. Conversely, the expression of the amino-terminal domain of DLC-1 acts as a dominant negative and profoundly inhibits cell migration by displacing endogenous DLC-1 from focal adhesions.
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Registered trials
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.