ArticleAmerican journal of hematology2019
MYH9-related disease mutations cause abnormal red blood cell morphology through increased myosin-actin binding at the membrane.
Article in American journal of hematology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- The membrane skeleton density of red blood cells in MYH9-related disease patients is decreased.Bioscience reports · 2026Article
- Article
- A case report of a family with MYH9 gene mutation-related disease in an ethnic minority group and literature review.BMC medical genomics · 2026Review
- Cancer-associated SF3B1 mutation suppresses DNA repair by disrupting the organization of nuclear actin network.Cell death & disease · 2026Article
- Nonmuscle myosin IIA (NMIIA) regulates anisotropic cell tension to maintain the hexagonal packing of mouse lens meridional row cells.Molecular biology of the cell · 2025Article
- Disease-related non-muscle myosin IIA D1424N rod domain mutation, but not R702C motor domain mutation, disrupts mouse ocular lens fiber cell alignment and hexagonal packing.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Article
- Article
- Exploring the nexus between MYH9 and tumors: novel insights and new therapeutic opportunities.Frontiers in cell and developmental biology · 2024Review
- A familial case of MYH9 gene mutation associated with multiple functional and structural platelet abnormalities.Scientific reports · 2022Article
- Identification of Transferrin Receptor 1 (TfR1) Overexpressed in Lung Cancer Cells, and Internalization of Magnetic Au-CoFePharmaceutics · 2022Article
- Reduced platelet forces underlie impaired hemostasis in mouse models ofScience advances · 2022Article
- Ruscogenin alleviates LPS-triggered pulmonary endothelial barrier dysfunction through targeting NMMHC IIA to modulate TLR4 signaling.Acta pharmaceutica Sinica. B · 2022Article
- Nanoscale dynamics of actin filaments in the red blood cell membrane skeleton.Molecular biology of the cell · 2022Article
- "CHildren with Inherited Platelet disorders Surveillance" (CHIPS) retrospective and prospective observational cohort study by Italian Association of Pediatric Hematology and Oncology (AIEOP).Frontiers in pediatrics · 2022Article
- MYH9 is crucial for stem cell-like properties in non-small cell lung cancer by activating mTOR signaling.Cell death discovery · 2021Article
- Three Signatures of Adaptive Polymorphism Exemplified by Malaria-Associated Genes.Molecular biology and evolution · 2021Article
- Article
- MYH9-related disease: it does exist, may be more frequent than you think and requires specific therapy.Clinical kidney journal · 2019Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
MYH9-related disease (MYH9-RD) is a rare, autosomal dominant disorder caused by mutations in MYH9, the gene encoding the actin-activated motor protein non-muscle myosin IIA (NMIIA). MYH9-RD patients suffer from bleeding syndromes, progressive kidney disease, deafness, and/or cataracts, but the impact of MYH9 mutations on other NMIIA-expressing tissues remains unknown. In human red blood cells (RBCs), NMIIA assembles into bipolar filaments and binds to actin filaments (F-actin) in the spectrin-F-actin membrane skeleton to control RBC biconcave disk shape and deformability. Here, we tested the effects of MYH9 mutations in different NMIIA domains (motor, coiled-coil rod, or non-helical tail) on RBC NMIIA function. We found that MYH9-RD does not cause clinically significant anemia and that patient RBCs have normal osmotic deformability as well as normal membrane skeleton composition and micron-scale distribution. However, analysis of complete blood count data and peripheral blood smears revealed reduced hemoglobin content and elongated shapes, respectively, of MYH9-RD RBCs. Patients with mutations in the NMIIA motor domain had the highest numbers of elongated RBCs. Patients with mutations in the motor domain also had elevated association of NMIIA with F-actin at the RBC membrane. Our findings support a central role for motor domain activity in NMIIA regulation of RBC shape and define a new sub-clinical phenotype of MYH9-RD.
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