ArticleStructure (London, England : 1993)2021
Structural Basis of CYRI-B Direct Competition with Scar/WAVE Complex for Rac1.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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
11 citing papers in PubMed, 18 citations in OpenAlex.
- Mechanical observables of cancer invasion: actin, adhesion, and metastatic plasticity.Frontiers in cell and developmental biology · 2026Review
- GαInternational journal of molecular sciences · 2025Article
- CYRI controls epidermal wound closure and cohesion of invasive border cell cluster in Drosophila.The Journal of cell biology · 2024Article
- CYRI-B-mediated macropinocytosis drives metastasis via lysophosphatidic acid receptor uptake.eLife · 2024Article
- PPP2R1A regulates migration persistence through the NHSL1-containing WAVE Shell Complex.Nature communications · 2023Article
- CYRI proteins: controllers of actin dynamics in the cellular 'eat vs walk' decision.Biochemical Society transactions · 2023Review
- Rac1: A Regulator of Cell Migration and a Potential Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023Review
- Regulation of the Scar/WAVE complex in migrating cells: A summary of our understanding.Journal of biosciences · 2023Review
- Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase.Nature communications · 2022Article
- Characterization and Functional Study ofGenes · 2022Article
- CYRI-A limits invasive migration through macropinosome formation and integrin uptake regulation.The Journal of cell biology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
Rac1 is a major regulator of actin dynamics, with GTP-bound Rac1 promoting actin assembly via the Scar/WAVE complex. CYRI competes with Scar/WAVE for interaction with Rac1 in a feedback loop regulating actin dynamics. Here, we reveal the nature of the CYRI-Rac1 interaction, through crystal structures of CYRI-B lacking the N-terminal helix (CYRI-BΔN) and the CYRI-BΔN:Rac1Q61L complex, providing the molecular basis for CYRI-B regulation of the Scar/WAVE complex. We reveal CYRI-B as having two subdomains - an N-terminal Rac1 binding subdomain with a unique Rac1-effector interface and a C-terminal Ratchet subdomain that undergoes conformational changes induced by Rac1 binding. Finally, we show that the CYRI protein family, CYRI-A and CYRI-B can produce an autoinhibited hetero- or homodimers, adding an additional layer of regulation to Rac1 signaling.
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What OpenQuestion holds
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.