Correction to: Histamine N-methyltransferase (HNMT) as a potential auxiliary biomarker for predicting adaptability to anti-HER2 drug treatment in breast cancer patients (Biomarker Research, (2025), 13, 1, (7), 10.1186/s40364-024-00715-5)

The authors discovered an issue in Fig. 5A in the original article whereby an editing error duplicated an image. The authors have identified the original data files and confirmed the correct version of the figure which can be viewed ahead in this Correction article. The molecular mechanism by which HNMT enhances BC cell sensitivity to anti-HER2 targeted drugs. The molecular mechanism underlying HER2-induced oncogenesis involves a series of intricate steps. A In this study, EGF (100 ng/mL) was added to SKBR3 cancer cells, and the kinetic process of complex formation was observed. (a) Firstly, in response to EGF activation of HER2 signaling, cytoplasmic HNMT translocates to the cell membrane, and the HNMT/HER2 complex can be observed on the cell membrane within approximately 10–20 min (red arrows). Following this, (b-c) HNMT facilitates the recruitment of γ-secretase, which occurs around 30 min. Subsequently, the γ-secretase (PS1/PS2) complex forms with HER2, taking approximately 30–60 min. During this process, the HER2-ICD enters the cytoplasm (white arrowhead). (d-e) After 60 min of EGF treatment, it is observable that the HNMT/HER2-ICD complex enters the cell nucleus (yellow arrow). It binds to the HER2 promoter, inducing the upregulation of HER2 and HER2-associated oncogenic proteins. The newly synthesized HER2 protein subsequently translocates to the cell membrane, contributing to the manifestation of an H-cell phenotype and enhancing the binding of therapeutic agents such as trastuzumab or T-Dxd in HER2+cells.