ArticleJournal of molecular biology2007
Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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Who cites it
80 citing papers in PubMed, 126 citations in OpenAlex.
- Septin crosstalk with microtubules and actin is regulated by a GSK3-dependent phosphoswitch.bioRxiv : the preprint server for biology · 2026Article
- The unphosphorylated, closed form of ezrin binds to RNA to maintain a metastatic phenotype in osteosarcoma cells.Science signaling · 2026Article
- T-cell-targeted immunotherapy in neurofibromatosis type 2-related vestibular schwannoma: current evidence and future direction.Brain communications · 2026Review
- Measuring and manipulating localized translation of erm-1 in the C. elegans embryo.Development (Cambridge, England) · 2025Article
- The Molecular Biology of Placental Transport of Calcium to the Human Foetus.International journal of molecular sciences · 2025Review
- Radixin: Roles in the Nervous System and Beyond.Biomedicines · 2024Review
- The molecular biology of NF2/Merlin on tumorigenesis and development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Review
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- A bipartite NLS motif mediates the nuclear import ofFrontiers in cell and developmental biology · 2024Article
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- The genetic landscape and possible therapeutics of neurofibromatosis type 2.Cancer cell international · 2023Review
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- Article
- Antisense oligonucleotides targeting exon 11 are able to partially rescue the NF2-related schwannomatosis phenotypeMolecular therapy. Nucleic acids · 2022Article
- The ERM-1 membrane-binding domain directs erm-1 mRNA localization to the plasma membrane in the C. elegans embryo.Development (Cambridge, England) · 2022Article
- Characterization of protein complexes in extracellular vesicles by intact extracellular vesicle crosslinking mass spectrometry (iEVXL).Journal of extracellular vesicles · 2022Article
- O-GlcNAcylation regulates lysophosphatidic acid-induced cell migration by regulating ERM family proteins.FEBS open bio · 2022Article
- Cotranslational interaction of human EBP50 and ezrin overcomes masked binding site during complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Contribution of protein-protein interactions to the endothelial-barrier-stabilizing function of KRIT1.Journal of cell science · 2022Article
- ERM-1 Phosphorylation and NRFL-1 Redundantly Control Lumen Formation in theFrontiers in cell and developmental biology · 2022Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
Ezrin/radixin/moesin (ERM) family members provide a regulated link between the cortical actin cytoskeleton and the plasma membrane to govern membrane structure and organization. Here, we report the crystal structure of intact insect moesin, revealing that its essential yet previously uncharacterized alpha-helical domain forms extensive interactions with conserved surfaces of the band four-point-one/ezrin/radixin/moesin (FERM) domain. These interdomain contacts provide a functional explanation for how PIP(2) binding and tyrosine phosphorylation of ezrin lead to activation, and provide an understanding of previously enigmatic loss-of-function missense mutations in the tumor suppressor merlin. Sequence conservation and biochemical results indicate that this structure represents a complete model for the closed state of all ERM-merlin proteins, wherein the central alpha-helical domain is an active participant in an extensive set of inhibitory interactions that can be unmasked, in a rheostat-like manner, by coincident regulatory factors that help determine cell polarity and membrane structure.
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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.