YWHAE

YWHAE is a gene that encodes for a protein known as 14-3-3 epsilon. This protein is a member of the 14-3-3 family of proteins, which play a significant role in signal transduction by binding to phosphoserine-containing proteins. The 14-3-3 proteins are highly conserved in eukaryotes and are involved in a wide range of cellular processes including cell cycle control, metabolism, and apoptosis.

Function[edit | edit source]

The YWHAE gene product, 14-3-3 epsilon, is involved in mediating signal transduction pathways. It achieves this by binding to a multitude of signaling proteins, thereby modulating their activity. For instance, 14-3-3 epsilon can bind to proteins involved in cell cycle regulation such as CDC25 phosphatases, influencing their ability to activate cyclin-dependent kinases and thus affecting cell cycle progression. Additionally, 14-3-3 epsilon plays a role in apoptosis by interacting with proteins like BAD and BAX, which are members of the Bcl-2 family involved in the regulation of programmed cell death.

Clinical Significance[edit | edit source]

Alterations in the YWHAE gene have been implicated in various human diseases. Deletions or mutations in YWHAE are associated with Miller-Dieker syndrome, a disorder characterized by lissencephaly (smooth brain) and craniofacial abnormalities. This association is due to YWHAE's location within the critical region of chromosome 17p13.3, which is deleted in patients with Miller-Dieker syndrome.

Furthermore, YWHAE has been studied in the context of cancer. Abnormal expression of 14-3-3 epsilon has been observed in several types of cancer, including breast cancer, lung cancer, and prostate cancer. Its role in cancer is complex, as it can act both as an oncogene and a tumor suppressor, depending on the cellular context and the nature of its interactions with other proteins.

Interaction with Other Proteins[edit | edit source]

YWHAE, through its product 14-3-3 epsilon, interacts with a wide array of proteins, reflecting its versatile role in cellular processes. These interactions are typically phosphoserine-dependent, meaning that 14-3-3 epsilon binds to its partners when they are phosphorylated on specific serine residues. This mode of interaction allows 14-3-3 epsilon to act as a scaffold protein, bringing together various components of signaling pathways and thereby coordinating complex cellular responses.