ArticleProceedings of the National Academy of Sciences of the United States of America2012
Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 63 citations in OpenAlex.
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- Structural and functional insights into TBC1D17 highlight the importance of the previously uncharacterized Rab-binding domain.Protein science : a publication of the Protein Society · 2026Article
- Control of lysosome function by the GTPase-activating protein TBC1D9B and its binding partner TMEM55B.Nature communications · 2026Article
- Endosome maturation is orchestrated by inside-out proton signaling through a NaResearch square · 2026Article
- A competition network connects Rab5 and Rab11 GTPases at the surface of endocytic structures.iScience · 2025Article
- Systematic characterization of all Toxoplasma gondii TBC domain-containing proteins identifies an essential regulator of Rab2 in the secretory pathway.PLoS biology · 2024Article
- Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation.Science advances · 2022Article
- Structural basis for the ARF GAP activity and specificity of the C9orf72 complex.Nature communications · 2021Article
- Rab29 Fast Exchange Mutants: Characterization of a Challenging Rab GTPase.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Multiple functions of TBCK protein in neurodevelopment disorders and tumors.Oncology letters · 2021Review
- Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation.ACS omega · 2020Review
- Ras-Specific GTPase-Activating Proteins-Structures, Mechanisms, and Interactions.Cold Spring Harbor perspectives in medicine · 2019Review
- Baicalein Targets GTPase-Mediated Autophagy to Eliminate Liver Tumor-Initiating Stem Cell-Like Cells Resistant to mTORC1 Inhibition.Hepatology (Baltimore, Md.) · 2018Article
- The tuberous sclerosis complex subunit TBC1D7 is stabilized by Akt phosphorylation-mediated 14-3-3 binding.The Journal of biological chemistry · 2018Article
- Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Small GTPases · 2018Review
- Article
- Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.Biochemistry · 2017Article
- Elucidation of Single Hydrogen Bonds in GTPases via Experimental and Theoretical Infrared Spectroscopy.Biophysical journal · 2017Article
- The identification of protein domains that mediate functional interactions between Rab-GTPases and RabGAPs using 3D protein modeling.Advances and applications in bioinformatics and chemistry : AABC · 2017Article
- Mechanism of the intrinsic arginine finger in heterotrimeric G proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rab GTPases, key regulators of vesicular transport, hydrolyze GTP very slowly unless assisted by Rab GTPase-activating proteins (RabGAPs). Dysfunction of RabGAPs is involved in many diseases. By combining X-ray structure analysis and time-resolved FTIR spectroscopy we reveal here the detailed molecular reaction mechanism of a complex between human Rab and RabGAP at the highest possible spatiotemporal resolution and in atomic detail. A glutamine residue of Rab proteins (cis-glutamine) that is essential for intrinsic activity is less important in the GAP-activated reaction. During generation of the RabGAP·Rab:GTP complex, there is a rapid conformational change in which the cis-glutamine is replaced by a glutamine from RabGAP (trans-glutamine); this differs from the RasGAP mechanism, where the cis-glutamine is also important for GAP catalysis. However, as in the case of Ras, a trans-arginine is also recruited to complete the active center during this conformational change. In contrast to the RasGAP mechanism, an accumulation of a state in which phosphate is bound is not observed, and bond breakage is the rate-limiting step. The movement of trans-glutamine and trans-arginine into the catalytic site and bond breakage during hydrolysis are monitored in real time. The combination of X-ray structure analysis and time-resolved FTIR spectroscopy provides detailed insight in the catalysis of human Rab GTPases.
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