ArticleThe Journal of biological chemistry2014
A WXW motif is required for the anticancer activity of the TAT-RasGAP317-326 peptide.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed, 23 citations in OpenAlex.
- Exploring the potential of anticancer peptides as therapeutic agents for cancer treatment.Research in pharmaceutical sciences · 2025Review
- Role of Anti-Cancer Peptides as Immunomodulatory Agents: Potential and Design Strategy.Pharmaceutics · 2022Review
- The EnvZ/OmpR Two-Component System Regulates the Antimicrobial Activity of TAT-RasGAPMicrobiology spectrum · 2022Article
- DLC1 Is a Prognosis-Related Biomarker Correlated With Tumor Microenvironment Remodeling in Endometrial Carcinoma.Frontiers in oncology · 2022Article
- Article
- TAT-RasGAPProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Anticancer peptide: Physicochemical property, functional aspect and trend in clinical application (Review).International journal of oncology · 2020Review
- ACPred: A Computational Tool for the Prediction and Analysis of Anticancer Peptides.Molecules (Basel, Switzerland) · 2019Article
- The Anticancer Peptide TAT-RasGAPFrontiers in microbiology · 2017Article
- The TAT-RasGAP317-326 anti-cancer peptide can kill in a caspase-, apoptosis-, and necroptosis-independent manner.Oncotarget · 2016Article
- Assessment of the chemosensitizing activity of TAT-RasGAP317-326 in childhood cancers.PloS one · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TAT-RasGAP317-326, a cell-permeable 10-amino acid-long peptide derived from the N2 fragment of p120 Ras GTPase-activating protein (RasGAP), sensitizes tumor cells to apoptosis induced by various anticancer therapies. This RasGAP-derived peptide, by targeting the deleted in liver cancer-1 (DLC1) tumor suppressor, also hampers cell migration and invasion by promoting cell adherence and by inhibiting cell movement. Here, we systematically investigated the role of each amino acid within the RasGAP317-326 sequence for the anticancer activities of TAT-RasGAP317-326. We report here that the first three amino acids of this sequence, tryptophan, methionine, and tryptophan (WMW), are necessary and sufficient to sensitize cancer cells to cisplatin-induced apoptosis and to reduce cell migration. The WMW motif was found to be critical for the binding of fragment N2 to DLC1. These results define the interaction mode between the active anticancer sequence of RasGAP and DLC1. This knowledge will facilitate the design of small molecules bearing the tumor-sensitizing and antimetastatic activities of TAT-RasGAP317-326.
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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.