SR protein: Difference between revisions

Latest revision as of 00:56, 28 February 2025

File:SR proteins translocation into and out of the nucleus.png

SR proteins translocation into and out of the nucleus

SR proteins are a family of RNA-binding proteins that are essential for splicing of pre-mRNA in eukaryotic cells. They are characterized by the presence of one or two RNA recognition motifs (RRMs) at the N-terminus and a C-terminal domain rich in serine and arginine residues, known as the RS domain.

Function[edit]

SR proteins play a crucial role in both constitutive splicing and alternative splicing of pre-mRNA. They are involved in the recognition of splice sites and the assembly of the spliceosome. SR proteins also participate in other aspects of RNA metabolism, including mRNA export, nonsense-mediated decay, and translation.

Structure[edit]

The structure of SR proteins typically includes:

One or two RRMs that bind to specific RNA sequences.
An RS domain that mediates protein-protein interactions and is subject to extensive phosphorylation.

Phosphorylation[edit]

Phosphorylation of the RS domain is critical for the function of SR proteins. It regulates their subcellular localization, interaction with other splicing factors, and activity in splicing. SR protein kinases (SRPKs) and Clk/Sty kinases are responsible for the phosphorylation of SR proteins.

Role in Disease[edit]

Dysregulation of SR proteins has been implicated in various diseases, including cancer, neurodegenerative disorders, and genetic diseases. Alterations in SR protein expression or function can lead to aberrant splicing and contribute to disease pathogenesis.

External links[edit]

[SR proteins at the Protein Data Bank]
[SR proteins in the Human Protein Atlas]

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-[[File:Protein SFRS9 PDB 1wg4.png|thumb]] [[File:SR proteins translocation into and out of the nucleus.png|thumb]] [[File:SR proteins competing with hnRNPs.png|thumb]] {{Short description|An overview of SR proteins and their role in RNA splicing}}
+[[File:Protein_SFRS9_PDB_1wg4.png|Protein SFRS9 PDB 1wg4|thumb]]
+[[File:SR_proteins_translocation_into_and_out_of_the_nucleus.png|SR proteins translocation into and out of the nucleus|thumb]]
+'''SR proteins''' are a family of [[RNA-binding proteins]] that are essential for [[splicing]] of pre-mRNA in [[eukaryotic cells]]. They are characterized by the presence of one or two [[RNA recognition motif|RNA recognition motifs]] (RRMs) at the N-terminus and a C-terminal domain rich in [[serine]] and [[arginine]] residues, known as the RS domain.
-'''SR proteins''' are a family of [[RNA-binding proteins]] that play a crucial role in the [[splicing]] of pre-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. The RS domain is essential for protein-protein interactions and for the recruitment of the splicing machinery.
+== Function ==
+SR proteins play a crucial role in both [[constitutive splicing]] and [[alternative splicing]] of pre-mRNA. They are involved in the recognition of [[splice sites]] and the assembly of the [[spliceosome]]. SR proteins also participate in other aspects of [[RNA metabolism]], including [[mRNA export]], [[nonsense-mediated decay]], and [[translation]].
-==Structure==
+== Structure ==
-SR proteins are defined by their modular structure, which typically includes:
+The structure of SR proteins typically includes:
+* One or two [[RNA recognition motif|RRMs]] that bind to specific [[RNA sequences]].
+* An RS domain that mediates protein-protein interactions and is subject to extensive [[phosphorylation]].
-* One or two RNA recognition motifs (RRMs) that bind to specific RNA sequences.
+== Phosphorylation ==
-* A C-terminal RS domain that is rich in serine and arginine residues. This domain is involved in protein-protein interactions and is often phosphorylated, which regulates the activity of the SR proteins.
+Phosphorylation of the RS domain is critical for the function of SR proteins. It regulates their subcellular localization, interaction with other splicing factors, and activity in splicing. [[SR protein kinases]] (SRPKs) and [[Clk/Sty kinases]] are responsible for the phosphorylation of SR proteins.
-==Function==
+== Role in Disease ==
-SR proteins are primarily involved in the regulation of [[alternative splicing]], a process that allows a single gene to produce multiple protein isoforms. They function by binding to [[exonic splicing enhancers]] (ESEs) and recruiting the [[spliceosome]] to the correct splice sites. This recruitment is crucial for the accurate removal of [[introns]] and the joining of [[exons]] in the pre-mRNA.
+Dysregulation of SR proteins has been implicated in various [[diseases]], including [[cancer]], [[neurodegenerative disorders]], and [[genetic diseases]]. Alterations in SR protein expression or function can lead to aberrant splicing and contribute to disease pathogenesis.
-===Role in Alternative Splicing===
+== See also ==
-Alternative splicing is a mechanism that increases the diversity of proteins that can be produced by a single gene. SR proteins influence this process by:
+* [[Spliceosome]]
-* Binding to ESEs and promoting the inclusion of specific exons.
-* Interacting with other splicing factors to modulate splice site selection.
-* Being involved in the regulation of splicing in response to cellular signals and conditions.
-===Phosphorylation===
-The activity of SR proteins is regulated by phosphorylation. The RS domain is a target for several kinases, including the [[SR protein kinases]] (SRPKs) and [[Clk/Sty kinases]]. Phosphorylation affects the localization, activity, and interactions of SR proteins, thereby influencing splicing outcomes.
-==Clinical Significance==
-Dysregulation of SR proteins has been implicated in various diseases, including cancer and neurodegenerative disorders. Mutations or altered expression of SR proteins can lead to aberrant splicing patterns, contributing to disease pathogenesis.
-==Research and Applications==
-SR proteins are a focus of research due to their central role in splicing and their potential as therapeutic targets. Modulating the activity of SR proteins or their phosphorylation status could provide new avenues for the treatment of diseases associated with splicing defects.
-==Also see==
-* [[RNA splicing]]
 * [[Alternative splicing]]
-* [[Spliceosome]]
 * [[RNA-binding protein]]
-* [[Exonic splicing enhancer]]
+* [[SR protein kinase]]
+== External links ==
+* [SR proteins at the Protein Data Bank]
+* [SR proteins in the Human Protein Atlas]
-{{RNA-binding proteins}}
+{{Protein-stub}}
-{{Splicing}}
 [[Category:RNA-binding proteins]]
+[[Category:Splicing factors]]
 [[Category:Gene expression]]
-[[Category:Molecular biology]]
+[[Category:Protein families]]