YTHDF2proteiinilla

YTHDF2 is a protein encoded in humans by the *YTHDF2* gene, located on chromosome 2 at position 2p23.3. It belongs to the YTH domain family of proteins, which are characterized by the presence of a YTH (YT521-B homology) domain. This domain is involved in the recognition of methylated RNA, specifically N6-methyladenosine (m6A), a common epigenetic modification found in both messenger RNA (mRNA) and non-coding RNAs.

YTHDF2 plays a critical role in post-transcriptional gene regulation by binding to m6A-modified RNAs. Its primary function is to promote the degradation of target mRNAs, thereby influencing gene expression levels. This process is particularly important in cellular differentiation, stress responses, and the maintenance of cellular homeostasis. Studies suggest that YTHDF2 contributes to various biological processes, including development, immune responses, and cancer progression.

In cancer biology, YTHDF2 has been implicated in tumor suppression and metastasis. For example, its expression is often downregulated in certain cancers, leading to the stabilization of oncogenic mRNAs and promoting tumor growth. Conversely, in other contexts, YTHDF2 may act as a tumor suppressor by degrading mRNAs that drive malignant phenotypes. The dual role of YTHDF2 highlights its complex regulatory functions and underscores the need for further research to fully understand its mechanisms.

Structurally, YTHDF2 consists of an N-terminal YTH domain and a C-terminal region that may facilitate interactions with other proteins or RNA-binding partners. Its activity is tightly regulated, often in coordination with other m6A-related proteins such as METTL3 (a methyltransferase) and FTO (a demethylase). Dysregulation of YTHDF2 has been linked to various diseases, including neurodegenerative disorders and metabolic disorders, in addition to cancer.

Research into YTHDF2 continues to expand, with ongoing studies exploring its potential as a therapeutic target in diseases where m6A modification is dysregulated. Understanding the precise functions and regulatory networks involving YTHDF2 could provide insights into novel treatment strategies.