Serine/arginine-rich splicing factor 10 (SFPQ), also known as PSF, is a multifunctional protein involved in various cellular processes, including transcription, RNA splicing, and DNA repair. Following its synthesis, SFPQ undergoes alterations that affect its structure and function. These changes can include phosphorylation, methylation, acetylation, or ubiquitination. For example, the addition of a phosphate group to specific amino acid residues can alter its interaction with other proteins or its localization within the cell.
These alterations are critical for regulating SFPQ’s diverse roles in the cell. They allow for dynamic control of its activity in response to cellular signals and environmental changes. Disruptions in these regulatory mechanisms have been implicated in several diseases, including neurodegenerative disorders and cancer, highlighting the importance of understanding the mechanisms controlling SFPQ function. The understanding of these processes has been historically crucial in unraveling the complexities of gene expression and cellular regulation.
