ArticlePloS one2014
The association of myosin IB with actin waves in dictyostelium requires both the plasma membrane-binding site and actin-binding region in the myosin tail.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- Reduced cell-substrate adhesion formation promotes cell migration inMolecular biology of the cell · 2025Article
- Reduced cell-substrate adhesion formation promotes cell migration inbioRxiv : the preprint server for biology · 2025Article
- Use of blue fluorescent protein Electra2 for live-cell imaging inmicroPublication biology · 2025Article
- Formation and closure of macropinocytic cups in Dictyostelium.Current biology : CB · 2023Article
- Article
- Dynamics of Actin Cytoskeleton and Their Signaling Pathways during Cellular Wound Repair.Cells · 2022Article
- The Amoebal Model for Macropinocytosis.Sub-cellular biochemistry · 2022Article
- Article
- Dictyostelium myosin 1F and myosin 1E inhibit actin waves in a lipid-binding-dependent and motor-independent manner.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Review
- Cell-Substrate Patterns Driven by Curvature-Sensitive Actin Polymerization: Waves and Podosomes.Cells · 2020Article
- Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization ofMolecular biology of the cell · 2020Article
- Actin Waves and Dynamic Patterning of the Plasma Membrane.The Yale journal of biology and medicine · 2019Article
- Membrane-cytoskeletal crosstalk mediated by myosin-I regulates adhesion turnover during phagocytosis.Nature communications · 2019Article
- Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes.Molecular biology of the cell · 2019Article
- Oscillatory Switches of Dorso-Ventral Polarity in Cells Confined between Two Surfaces.Biophysical journal · 2018Article
- Myosin 1b promotes axon formation by regulating actin wave propagation and growth cone dynamics.The Journal of cell biology · 2018Article
- MyTH4-FERM myosins have an ancient and conserved role in filopod formation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- ERK signaling promotes cell motility by inducing the localization of myosin 1E to lamellipodial tips.The Journal of cell biology · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
F-actin structures and their distribution are important determinants of the dynamic shapes and functions of eukaryotic cells. Actin waves are F-actin formations that move along the ventral cell membrane driven by actin polymerization. Dictyostelium myosin IB is associated with actin waves but its role in the wave is unknown. Myosin IB is a monomeric, non-filamentous myosin with a globular head that binds to F-actin and has motor activity, and a non-helical tail comprising a basic region, a glycine-proline-glutamine-rich region and an SH3-domain. The basic region binds to acidic phospholipids in the plasma membrane through a short basic-hydrophobic site and the Gly-Pro-Gln region binds F-actin. In the current work we found that both the basic-hydrophobic site in the basic region and the Gly-Pro-Gln region of the tail are required for the association of myosin IB with actin waves. This is the first evidence that the Gly-Pro-Gln region is required for localization of myosin IB to a specific actin structure in situ. The head is not required for myosin IB association with actin waves but binding of the head to F-actin strengthens the association of myosin IB with waves and stabilizes waves. Neither the SH3-domain nor motor activity is required for association of myosin IB with actin waves. We conclude that myosin IB contributes to anchoring actin waves to the plasma membranes by binding of the basic-hydrophobic site to acidic phospholipids in the plasma membrane and binding of the Gly-Pro-Gln region to F-actin in the wave.
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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.