U2AF2

From WikiMD's Wellness Encyclopedia


Overview[edit | edit source]

U2AF2 (U2 small nuclear RNA auxiliary factor 2) is a protein that in humans is encoded by the U2AF2 gene. It is a crucial component of the spliceosome, the complex responsible for the removal of introns from pre-mRNA in the process of RNA splicing. U2AF2 plays a significant role in the recognition of the 3' splice site during the early stages of spliceosome assembly.

Structure[edit | edit source]

U2AF2 is a member of the U2 auxiliary factor family and is characterized by its RNA recognition motifs (RRMs). The protein typically contains two RRMs that facilitate its binding to the polypyrimidine tract of the pre-mRNA. This binding is essential for the recruitment of the U2 snRNP to the branch point sequence, a critical step in spliceosome assembly.

Function[edit | edit source]

The primary function of U2AF2 is to assist in the accurate and efficient splicing of pre-mRNA. It acts as a bridge between the polypyrimidine tract and the U2 snRNP, ensuring the correct positioning of the spliceosome components. This interaction is vital for the recognition of the 3' splice site and the subsequent catalytic steps of splicing.

U2AF2 also interacts with other splicing factors, such as U2AF1, which binds to the AG dinucleotide at the 3' end of the intron. Together, U2AF1 and U2AF2 form a heterodimer that stabilizes the binding of the U2 snRNP to the pre-mRNA.

Clinical Significance[edit | edit source]

Mutations or dysregulation of U2AF2 have been implicated in various diseases, including certain types of cancer. Aberrant splicing due to malfunctioning U2AF2 can lead to the production of abnormal proteins that contribute to tumorigenesis. Understanding the role of U2AF2 in splicing can provide insights into potential therapeutic targets for splicing-related disorders.

Research and Studies[edit | edit source]

Recent studies have focused on the structural analysis of U2AF2 and its interactions with other splicing factors. Advanced techniques such as X-ray crystallography and cryo-electron microscopy have been employed to elucidate the molecular details of U2AF2's function. These studies aim to provide a comprehensive understanding of the splicing mechanism and the role of U2AF2 in this process.

Also see[edit | edit source]

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Contributors: Prab R. Tumpati, MD