SR protein
SR proteins are a family of RNA-binding proteins that play a crucial role in RNA splicing, a process essential for the maturation of messenger RNA (mRNA) in eukaryotic cells. These proteins are characterized by the presence of one or two RNA recognition motifs (RRMs) at their N-terminus and a C-terminal domain rich in serine and arginine residues, known as the RS domain.
Structure[edit | edit source]
SR proteins typically contain:
- One or two RNA recognition motifs (RRMs) at the N-terminus.
- A C-terminal domain rich in serine and arginine residues, known as the RS domain.
Function[edit | edit source]
SR proteins are involved in multiple steps of the RNA splicing process, including:
- Spliceosome assembly
- Splice site selection
- Regulation of alternative splicing
They also play roles in other aspects of RNA metabolism, such as mRNA export, nonsense-mediated decay, and translation.
Mechanism[edit | edit source]
SR proteins function by binding to exonic splicing enhancers (ESEs) within the pre-mRNA. This binding facilitates the recruitment of the spliceosome components to the correct splice sites, ensuring accurate and efficient splicing.
Regulation[edit | edit source]
The activity of SR proteins is regulated by phosphorylation of their RS domain. Kinases such as SRPK1 and CLK1 phosphorylate SR proteins, modulating their interaction with other splicing factors and RNA.
Clinical Significance[edit | edit source]
Mutations or dysregulation of SR proteins have been implicated in various diseases, including:
List of SR Proteins[edit | edit source]
Some well-known SR proteins include:
Related Pages[edit | edit source]
References[edit | edit source]
External Links[edit | edit source]
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Contributors: Prab R. Tumpati, MD