ArticleOncogene1999
Expression level, subcellular distribution and rho-GDI binding affinity of merlin in comparison with Ezrin/Radixin/Moesin proteins.
Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 85 citations in OpenAlex.
- Article
- Morphological control of merlin-Rac antagonism in proliferation-promoting signaling.Science signaling · 2025Article
- RhoGDI in RBL-2H3 cells acts as a negative regulator of Rho GTPase signaling to inhibit granule exocytosis.Journal of leukocyte biology · 2024Article
- Electrostatic Forces Mediate the Specificity of RHO GTPase-GDI Interactions.International journal of molecular sciences · 2021Article
- EphrinB1 promotes cancer cell migration and invasion through the interaction with RhoGDI1.Oncogene · 2018Article
- Ezrin-expressing lung adenocarcinoma cells and podoplanin-positive fibroblasts form a malignant microenvironment.Journal of cancer research and clinical oncology · 2015Article
- A neuronal function of the tumor suppressor protein merlin.Acta neuropathologica communications · 2014Review
- Conserved sequence repeats of IQGAP1 mediate binding to Ezrin.Journal of proteome research · 2014Article
- Merlin isoform 2 in neurofibromatosis type 2-associated polyneuropathy.Nature neuroscience · 2013Article
- Quantitative analysis of prenylated RhoA interaction with its chaperone, RhoGDI.The Journal of biological chemistry · 2012Article
- Molecular mechanisms promoting the pathogenesis of Schwann cell neoplasms.Acta neuropathologica · 2012Review
- Phosphorylation of podocalyxin (Ser415) Prevents RhoA and ezrin activation and disrupts its interaction with the actin cytoskeleton.The American journal of pathology · 2011Article
- Apical membrane segregation of phosphatidylinositol-4,5-bisphosphate influences parathyroid hormone 1 receptor compartmental signaling and localization via direct regulation of ezrin in LLC-PK1 cells.Cellular signalling · 2011Article
- The 'invisible hand': regulation of RHO GTPases by RHOGDIs.Nature reviews. Molecular cell biology · 2011Review
- Merlin, a "magic" linker between extracellular cues and intracellular signaling pathways that regulate cell motility, proliferation, and survival.Current protein & peptide science · 2010Review
- Organizing the cell cortex: the role of ERM proteins.Nature reviews. Molecular cell biology · 2010Review
- Merlin and the ERM proteins--regulators of receptor distribution and signaling at the cell cortex.Trends in cell biology · 2009Review
- Localization to the cortical cytoskeleton is necessary for Nf2/merlin-dependent epidermal growth factor receptor silencing.Molecular and cellular biology · 2008Article
- Modeling NF2 with human arachnoidal and meningioma cell culture systems: NF2 silencing reflects the benign character of tumor growth.Neurobiology of disease · 2008Article
- Temporal control of Rac in Schwann cell-axon interaction is disrupted in NF2-mutant schwannoma cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Merlin, a neurofibromatosis type-2 tumor suppressor, shows significant sequence similarity to ERM (Ezrin/Radixin/Moesin) proteins, general actin filament/plasma membrane cross-linkers, which are regulated in a Rho-dependent manner. To understand its physiological functions, we compared merlin with ERM proteins in vivo and in vitro. Quantitative immunoblotting revealed that the molar ratio of merlin/ERM in cultured epithelial or non-epithelial cells was approximately 0.14 or approximately 0.05, respectively. After centrifugation of cell homogenate, merlin was mostly recovered in the insoluble fraction, whereas almost half of ERM proteins were found in the soluble fraction. Merlin and ERM proteins were concentrated at microvilli when introduced into fibroblasts. In contrast, in epithelial cells, introduced merlin was co-distributed with E-cadherin in lateral membranes, whereas ERM proteins were concentrated in apical microvilli. Finally, we examined the binding affinity of merlin to Rho GDP dissociation inhibitor (Rho-GDI), to which N-terminal halves of ERM proteins but not the full-length molecules specifically bind. In vitro binding assays revealed that the N-terminal halves of merlin isoform-I and -II as well as full-length merlin isoform-II bound to Rho-GDI with similar binding affinity to ERM proteins. Immunoprecipitation confirmed these findings in vivo. These findings do not favor the notion that merlin functions simply in a redundant or competitive manner to ERM proteins.
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