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|Protein SFRS9 PDB 1wg4]] [[file:SR_proteins_translocation_into_and_out_of_the_nucleus.png|thumb|SR proteins translocation into and out of the nucleus|left]] [[file:SR_proteins_competing_with_hnRNPs.png|thumb|SR proteins competing with hnRNPs]] '''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.
+[[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.
-==Structure==
+== Function ==
-SR proteins typically contain:
+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]].
-* 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==
+== Structure ==
-SR proteins are involved in multiple steps of the [[RNA splicing]] process, including:
+The structure of SR proteins typically includes:
-* [[Spliceosome]] assembly
+* One or two [[RNA recognition motif|RRMs]] that bind to specific [[RNA sequences]].
-* Splice site selection
+* An RS domain that mediates protein-protein interactions and is subject to extensive [[phosphorylation]].
-* Regulation of alternative splicing
-They also play roles in other aspects of RNA metabolism, such as [[mRNA export]], [[nonsense-mediated decay]], and [[translation]].
+== Phosphorylation ==
+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.
-==Mechanism==
+== Role in Disease ==
-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.
+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.
-==Regulation==
+== See also ==
-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==
-Mutations or dysregulation of SR proteins have been implicated in various diseases, including:
-* [[Cancer]]
-* [[Spinal muscular atrophy]]
-* [[Myotonic dystrophy]]
-==List of SR Proteins==
-Some well-known SR proteins include:
-* [[SRSF1]]
-* [[SRSF2]]
-* [[SRSF3]]
-* [[SRSF4]]
-* [[SRSF5]]
-==Related Pages==
-* [[RNA splicing]]
 * [[Spliceosome]]
+* [[Alternative splicing]]
 * [[RNA-binding protein]]
-* [[Exonic splicing enhancer]]
+* [[SR protein kinase]]
-* [[Phosphorylation]]
-==References==
+== External links ==
-{{Reflist}}
+* [SR proteins at the Protein Data Bank]
+* [SR proteins in the Human Protein Atlas]
-==External Links==
+{{Protein-stub}}
-{{Commons category|SR proteins}}
 [[Category:RNA-binding proteins]]
-[[Category:RNA splicing]]
+[[Category:Splicing factors]]
 [[Category:Gene expression]]
 [[Category:Protein families]]
-[[Category:Cell biology]]
-{{medicine-stub}}