ArticleProceedings of the National Academy of Sciences of the United States of America2011
Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
39 citing papers in PubMed, 70 citations in OpenAlex.
- Spindle-localized F-actin regulates polar MTOC organization and the fidelity of meiotic spindle formation.Nature communications · 2025Article
- Cell-particles interaction - selective uptake and transport of microdiamonds.Communications biology · 2024Article
- Myosin-X recruits lamellipodin to filopodia tips.Journal of cell science · 2023Article
- Myosin-X and talin modulate integrin activity at filopodia tips.Cell reports · 2021Article
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- The netrin receptor UNC-40/DCC assembles a postsynaptic scaffold and sets the synaptic content of GABANature communications · 2020Article
- Phenotypic analysis of Myo10 knockout (Myo10Scientific reports · 2019Article
- An interaction between myosin-10 and the cell cycle regulator Wee1 links spindle dynamics to mitotic progression in epithelia.The Journal of cell biology · 2018Article
- Revisiting Netrin-1: One Who Guides (Axons).Frontiers in cellular neuroscience · 2018Review
- The binding of DCC-P3 motif and FAK-FAT domain mediates the initial step of netrin-1/DCC signaling for axon attraction.Cell discovery · 2018Article
- Structural basis of kindlin-mediated integrin recognition and activation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Myosin 7 and its adaptors link cadherins to actin.Nature communications · 2017Article
- Structure of Myo7b/USH1C complex suggests a general PDZ domain binding mode by MyTH4-FERM myosins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions.Current opinion in cell biology · 2017Review
- The Janus Kinase (JAK) FERM and SH2 Domains: Bringing Specificity to JAK-Receptor Interactions.Frontiers in endocrinology · 2017Review
- 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
- A Combination of Diffusion and Active Translocation Localizes Myosin 10 to the Filopodial Tip.The Journal of biological chemistry · 2016Article
- Myosin-10 independently influences mitotic spindle structure and mitotic progression.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin X (MyoX), encoded by Myo10, is a representative member of the MyTH4-FERM domain-containing myosins, and this family of unconventional myosins shares common functions in promoting formation of filopodia/stereocilia structures in many cell types with unknown mechanisms. Here, we present the structure of the MyoX MyTH4-FERM tandem in complex with the cytoplasmic tail P3 domain of the netrin receptor DCC. The structure, together with biochemical studies, reveals that the MyoX MyTH4 and FERM domains interact with each other, forming a structural and functional supramodule. Instead of forming an extended β-strand structure in other FERM binding targets, DCC_P3 forms a single α-helix and binds to the αβ-groove formed by β5 and α1 of the MyoX FERM F3 lobe. Structure-based amino acid sequence analysis reveals that the key polar residues forming the inter-MyTH4/FERM interface are absolutely conserved in all MyTH4-FERM tandem-containing proteins, suggesting that the supramodular nature of the MyTH4-FERM tandem is likely a general property for all MyTH4-FERM proteins.
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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.