ArticleScientific reports2017
A conformational change within the WAVE2 complex regulates its degradation following cellular activation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- SLC7A11-mediated cystine accumulation and Rac1-WRC-Arp2/3-driven actin cytoskeletal folding synergistically induce disulfidptosis in acute myocardial infarction.Communications biology · 2026Article
- WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation.The Journal of cell biology · 2025Article
- PPP2R1A regulates migration persistence through the NHSL1-containing WAVE Shell Complex.Nature communications · 2023Article
- Article
- Hypermethylated WASF2: tumor suppressive role in head and neck squamous cell carcinoma.Translational cancer research · 2023Article
- Regulation of the Scar/WAVE complex in migrating cells: A summary of our understanding.Journal of biosciences · 2023Review
- TMEM123 a key player in immune surveillance of colorectal cancer.Frontiers in immunology · 2023Article
- Targeting the WASF3 complex to suppress metastasis.Pharmacological research · 2022Review
- CK1α protects WAVE from degradation to regulate cell shape and motility in the immune response.Journal of cell science · 2021Article
- Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration.Nature communications · 2021Article
- Targeting the actin nucleation promoting factor WASp provides a therapeutic approach for hematopoietic malignancies.Nature communications · 2021Article
- The Bardet-Biedl syndrome complex component BBS1 controls T cell polarity during immune synapse assembly.Journal of cell science · 2021Article
- Review
- CBeLife · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
WASp family Verprolin-homologous protein-2 (WAVE2), a member of the Wiskott-Aldrich syndrome protein (WASp) family of actin nucleation promoting factors, is a central regulator of actin cytoskeleton polymerization and dynamics. Multiple signaling pathways operate via WAVE2 to promote the actin-nucleating activity of the actin-related protein 2/3 (Arp2/3) complex. WAVE2 exists as a part of a pentameric protein complex known as the WAVE regulatory complex (WRC), which is unstable in the absence of its individual proteins. While the involvement of WAVE2 in actin polymerization has been well documented, its negative regulation mechanism is poorly characterized to date. Here, we demonstrate that WAVE2 undergoes ubiquitylation in a T-cell activation dependent manner, followed by proteasomal degradation. The WAVE2 ubiquitylation site was mapped to lysine 45, located at the N-terminus where WAVE2 binds to the WRC. Using Förster resonance energy transfer (FRET), we reveal that the autoinhibitory conformation of the WRC maintains the stability of WAVE2 in resting cells; the release of autoinhibition following T-cell activation facilitates the exposure of WAVE2 to ubiquitylation, leading to its degradation. The dynamic conformational structures of WAVE2 during cellular activation dictate its degradation.
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