MYH9 (Myosin Heavy Chain 9)

This review aims to present the structure, functional significance, and clinical associations of MYH9, with an emphasis on its contributions to MYH9-RD and cancer progression. Furthermore, it examines MYH9's regulatory interactions with non-coding RNAs and its potential applications as a therapeutic target, offering insights into strategies such as RNA interference and CRISPR-based gene editing for cancer treatment.

Cisplatin treatment induces KIF23 expression in a concentration- and time-dependent manner. KIF23 recruits USP7, which removes the K48-linked ubiquitin chain of MYH9, thereby stabilising MYH9 and facilitating its nuclear transport. MYH9 recruits USP15, thereby stabilising MCM2, which, in turn, regulates the G1/S phase transition by binding to PCNA. Targeting the KIF23/MYH9/MCM2/PCNA axis sensitises cervical cancer cells to cisplatin.

MYH9 acts as an oncogenic gene in SCC, which promotes the carcinogenesis and progression of SCC cells via EMT signaling, and it may serve as a valuable patent for targeted treatment biomarker of SCC.

Collectively, these results suggest that OTUD4 functions as a tumor suppressor in prostate cancer. Specifically, OTUD4 inhibits MYH9 degradation via deubiquitination, thereby enabling MYH9-mediated suppression of prostate cancer.

Collectively, p40 is an initial signal for squamous metaplasia development from morular and Sur Ca cells, by modulating CSC properties. This leads to terminal squamous differentiation through the MYH9 monomer-polymer equilibrium, regulated by EBP50 and S100A4 under hypoxic conditions.

This stabilizes the MYH9 protein by preventing its degradation through the ubiquitin-proteasome pathway and further activates the AKT/BAD signaling axis, ultimately suppressing apoptosis and conferring lenvatinib resistance. Implications: Targeting the ETS1/USP43/MYH9 axis presents a promising therapeutic strategy to overcome lenvatinib resistance in HCC.

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.