ArticleProceedings of the National Academy of Sciences of the United States of America2013
Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- The C2 domain augments Ras GTPase-activating protein catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rasal1 regulates calcium dependent neuronal maturation by modifying microtubule dynamics.Cell & bioscience · 2024Article
- Analysis of the Guanine Nucleotide-Bound State of KRAS by Ion-Pair Reversed-Phase High-Performance Liquid Chromatography.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Who's in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond.The Journal of cell biology · 2021Review
- RASAL3 Is a Putative RasGAP Modulating Inflammatory Response by Neutrophils.Frontiers in immunology · 2021Article
- Role of RASA1 in cancer: A review and update (Review).Oncology reports · 2020Review
- Differential effects of RASA3 mutations on hematopoiesis are profoundly influenced by genetic background and molecular variant.PLoS genetics · 2020Article
- The Cytosolic Phospholipase ABiomolecules · 2020Article
- A gravitropic stimulus alters the distribution of EHB1, a negative effector of root gravitropism in Arabidopsis.Plant direct · 2020Article
- GTPase-activating protein Rasal1 associates with ZAP-70 of the TCR and negatively regulates T-cell tumor immunity.Nature communications · 2019Article
- Ras-Specific GTPase-Activating Proteins-Structures, Mechanisms, and Interactions.Cold Spring Harbor perspectives in medicine · 2019Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- From Ras to Rap and Back, a Journey of 35 Years.Cold Spring Harbor perspectives in medicine · 2018Review
- Complement Receptor 3-Mediated Inhibition of Inflammasome Priming by Ras GTPase-Activating Protein DuringFrontiers in immunology · 2018Article
- GPCR-controlled membrane recruitment of negative regulator C2GAP1 locally inhibits Ras signaling for adaptation and long-range chemotaxis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1.Nature communications · 2017Article
- RAS Promotes Proliferation and Resistances to Apoptosis in Meningioma.Molecular neurobiology · 2017Article
- Insights into the inhibitory mechanism of triazole-based small molecules on phosphatidylinositol-4,5-bisphosphate binding pleckstrin homology domain.Biochemistry and biophysics reports · 2015Article
- Identification of a Rab GTPase-activating protein cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rasal, belonging to the GAP1 subfamily of Ras GTPase-activating proteins (RasGAPs) with dual RasGAP/RapGAP specificity, is epigenetically silenced in several tumor types. Surprisingly, the isolated protein has GAP activity on Rap but not on Ras. Its membrane recruitment is regulated by interaction with calcium and lipids, which simultaneously induces its RasGAP activity through a yet unknown mechanism. Here we show that the interaction of Rasal with membranes induces Rasal RasGAP activity by spatial and conformational regulation, although it does not have any effect on its RapGAP activity. Not only is colocalization of Rasal and Ras in the membrane essential for RasGAP activation, but direct and Ca-dependent interaction between the tandem C2 domains of Rasal and lipids of the membrane is also required. Whereas the C2A domain binds specifically phosphatidylserine, the C2B domain interacts with several phosphoinositol lipids. Finally we show, that similar to the C2 domains of synaptotagmins, the Rasal tandem C2 domains are able to sense and induce membrane curvature by the insertion of hydrophobic loops into the membrane.
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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.