MYH9 (Myosin Heavy Chain 9)

This study established CD133+ CSCs as critical mediators through the CD133-MYH9/β-catenin axis in MASLD-HCC. Targeting CD133 enhances multikinase inhibitor efficacy, offering a promising therapeutic strategy for MASLD-HCC.

This article introduces the characteristics of myosin superfamily members and systematically reviews the structure, regulation and physiological functions of MYH9 and NMIIA, as well as MYH9-related disorders (MYH9-RD) caused by MYH9 mutations, focusing on the role of NMIIA in the pathogenesis of various cancers, and summarizes the therapeutic mechanisms of its targeted drugs. Besides, the effects of NMIIA in neurological diseases and infectious diseases are discussed to provide a comprehensive theoretical basis and insights for MYH9 and NMIIA as a therapeutic target for multiple diseases.

A large-scale drug screen of 786 Food and Drug Administration (FDA)-approved anticancer agents identified the acridine compound amsacrine hydrochloride as a potent inhibitor of PDOs and cell lines...This inhibition disrupts the PI3K/ERK/FOXO/PLK1 signaling pathway and attenuates KRAS-driven hypertranscription. In conclusion, the acridine derivative LS-1-2 emerges as a promising candidate from this preclinical investigation, providing a rationale for future clinical trials in KRAS-mutant CRC.

This is the first Romanian pediatric cohort and one of the few existing pediatric cohorts describing the genetic and clinical spectrum of MYH9-RD. Early genetic confirmation enables precise diagnosis, tailored management, and family screening, while preventing inappropriate therapies.

A novel mutation of MYH9 was found in this study, and the case was sensitive to Avatrombopag, by exploring the relationship between the MYH9 gene and tumors, suggesting that the MYH9 gene may be associated with the development of diffuse large B-cell lymphoma.

Co-expression networks and integrative analyses further reinforced these distinctions, uncovering coordinated protein-metabolite modules. Our findings reveal novel, subtype-specific molecular programs in RMS and propose candidate biomarkers and pathways that may guide precision diagnostics and therapeutic targeting in pediatric sarcomas.

This comprehensive review synthesizes the current body of knowledge regarding MYH9's role in GI tumors, focusing on its molecular mechanisms, including its interaction with key signaling pathways like the phosphatidylinositol 3-kinase/protein kinase B/mechanistic target of rapamycin axis, which suggests a role in cancer cell survival, proliferation, and epithelial-mesenchymal transition. The review also explores MYH9's potential as a therapeutic target, with preclinical models demonstrating promising results in inhibiting tumor growth and enhancing chemosensitivity. The evidence suggests that MYH9 is a multifaceted protein with significant implications in GI tumor biology, warranting further research to elucidate its mechanisms of action and develop targeted therapies that could improve patient outcomes.

PGK1 promotes ESCC tumourigenicity and migratory capacity by facilitating β-catenin-dependent c-Myc transcription. Under hypoxic conditions, the PGK1‒MYH9 interaction is strengthened, and HIF-1α-mediated transcription increases PGK1 expression, thereby activating the β-catenin/c-Myc signalling pathway. Taken together, PGK1 holds promise as a potential biomarker for predicting postoperative prognosis and recurrence in patients with ESCC.

Additionally, the RNA-binding protein insulin-like growth factor 2 mRNA-binding protein 2 binds to LINC02820 and increase its RNA stability in ESCC cells, thus upregulating LINC02820 expression. Therefore, these findings indicate LINC02820 as an oncogenic lncRNA in ESCC progression and suggest its potential as a therapeutic target.

siRNA-mediated depletion of NMHCIIA from FLO-1 cells altered cell morphology, gave rise to an increased number of stress fibre like structures and reduced FLO-1 cell migration. These findings suggest that NMHCIIA influences FLO-1 cell migration by regulating F-actin dynamics and the actin cytoskeleton, providing insight into the mechanisms of migration employed by OAC cells and identifying NMHCIIA as a potential therapeutic target for this disease.