SERF2 Human

Small EDRK-Rich Factor 2 (SERF2) is a highly conserved protein that plays a significant role in the regulation of amyloid protein aggregation and proteotoxicity. This protein is encoded by the SERF2 gene and is involved in various cellular processes, including protein destabilization and stress response. The recombinant form of SERF2, produced through genetic engineering techniques, allows for detailed study and application in research and therapeutic contexts.

SERF2 is characterized by its rich content of the amino acids glutamic acid (E), aspartic acid (D), arginine ®, and lysine (K). This composition contributes to its ability to interact with other proteins and nucleic acids. SERF2 is known to induce conformational changes in amyloid proteins, driving them into compact formations that precede the formation of aggregates . This activity is crucial in understanding the mechanisms of protein aggregation, which is a hallmark of several neurodegenerative diseases.

SERF2 positively regulates the aggregation of amyloid proteins, such as mutant huntingtin (HTT) in Huntington’s disease, α-synuclein in Parkinson’s disease, and amyloid-beta (Aβ) in Alzheimer’s disease . The aggregation process is believed to be a cellular protection mechanism against cytotoxic intermediates that arise during protein misfolding. By promoting the formation of aggregates, SERF2 helps to mitigate the toxic effects of these intermediates.

Research involving SERF2 has been facilitated by the development of knockout mouse models. These models have provided insights into the role of SERF2 in regulating age-related proteotoxicity and other physiological processes . For instance, studies have shown that SERF2 knockout mice exhibit developmental deficits and altered stress responses, highlighting the importance of SERF2 in normal cellular function.

Recent studies have revealed that SERF2 binds specifically to non-canonical RNA structures known as G-quadruplexes. This interaction plays a significant role in the formation of stress granules, which are aggregates of proteins and RNAs that form in response to cellular stress . The depletion of SERF2 has been shown to significantly affect the size and abundance of stress granules, indicating its crucial role in the cellular stress response.

The recombinant form of SERF2 is valuable in research settings, allowing scientists to study its function and interactions in detail. Understanding the mechanisms by which SERF2 regulates protein aggregation and stress response can lead to the development of therapeutic strategies for neurodegenerative diseases and other conditions associated with protein misfolding.