ArticleInternational journal of molecular sciences2021
Arpin Regulates Migration Persistence by Interacting with Both Tankyrases and the Arp2/3 Complex.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Ubiquitylation-dependent Rap2 activation regulates lamellipodia dynamics during cell migration.Journal of cell science · 2025Article
- Vinculin-Arp2/3 interaction inhibits branched actin assembly to control migration and proliferation.Life science alliance · 2025Article
- NHSL3 controls single and collective cell migration through two distinct mechanisms.Nature communications · 2025Article
- Regulation of Biomolecular Condensates by Poly(ADP-ribose).Chemical reviews · 2023Review
- PPP2R1A regulates migration persistence through the NHSL1-containing WAVE Shell Complex.Nature communications · 2023Article
- A Rab-bit hole: Rab40 GTPases as new regulators of the actin cytoskeleton and cell migration.Frontiers in cell and developmental biology · 2023Review
- An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases.Biomolecules · 2022Article
- Molecular mechanism of Arp2/3 complex inhibition by Arpin.Nature communications · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
During cell migration, protrusion of the leading edge is driven by the polymerization of Arp2/3-dependent branched actin networks. Migration persistence is negatively regulated by the Arp2/3 inhibitory protein Arpin. To better understand Arpin regulation in the cell, we looked for its interacting partners and identified both Tankyrase 1 and 2 (TNKS) using a yeast two-hybrid screening and coimmunoprecipitation with full-length Arpin as bait. Arpin interacts with ankyrin repeats of TNKS through a C-terminal-binding site on its acidic tail, which overlaps with the Arp2/3-binding site. Arpin was found to dissolve the liquid-liquid phase separation of TNKS upon overexpression. To uncouple the interactions of Arpin with TNKS and Arp2/3, we introduced point mutations in the Arpin tail and attempted to rescue the increased migration persistence of the Arpin knockout cells using random plasmid integration or compensating knock-ins at the
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