SRSF3 Gene

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SRSF3 Gene

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SRSF3 Gene

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">SRSF3 Gene</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>SRSF3</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Serine/Arginine-Rich Splicing Factor 3</td>
</tr>
<tr>
<td class="label">Alternative Names</td>
<td>SRp20, ASF/SF3</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>6p21.33</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6734</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000161547</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P84104</td>
</tr>
<tr>
<td class="label">Protein Class</td>
<td>RNA-binding protein; Splicing factor</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>ALS, Alzheimer's disease, Parkinson's disease, cancer</td>
</tr>
<tr>
<td class="label">Approach</td>
<td>Mechanism</td>
</tr>
<tr>
<td class="label">ASO therapy</td>
<td>Restore proper SRSF3 splicing patterns</td>
</tr>
<tr>
<td class="label">SRPK inhibitors</td>
<td>Modulate SRSF3 phosphorylation</td>
</tr>
<tr>
<td class="label">Small molecule modulators</td>
<td>Direct SRSF3 targeting</td>
</tr>
</table>

...

SRSF3 Gene

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">SRSF3 Gene</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>SRSF3</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Serine/Arginine-Rich Splicing Factor 3</td>
</tr>
<tr>
<td class="label">Alternative Names</td>
<td>SRp20, ASF/SF3</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>6p21.33</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6734</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000161547</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P84104</td>
</tr>
<tr>
<td class="label">Protein Class</td>
<td>RNA-binding protein; Splicing factor</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>ALS, Alzheimer's disease, Parkinson's disease, cancer</td>
</tr>
<tr>
<td class="label">Approach</td>
<td>Mechanism</td>
</tr>
<tr>
<td class="label">ASO therapy</td>
<td>Restore proper SRSF3 splicing patterns</td>
</tr>
<tr>
<td class="label">SRPK inhibitors</td>
<td>Modulate SRSF3 phosphorylation</td>
</tr>
<tr>
<td class="label">Small molecule modulators</td>
<td>Direct SRSF3 targeting</td>
</tr>
</table>

SRSF3 (Serine/Arginine-Rich Splicing Factor 3), also known as SRp20, is an essential RNA-binding protein that plays critical roles in pre-mRNA splicing, alternative splicing regulation, mRNA export, and translation. Located on chromosome 6p21.33, SRSF3 is the smallest member of the serine/arginine (SR) family of splicing factors. Dysregulation of SRSF3 has been implicated in [amyotrophic lateral sclerosis](/diseases/amyotrophic-lateral-sclerosis) (ALS), [Alzheimer's disease](/diseases/alzheimers-disease), [Parkinson's disease](/diseases/parkinsons-disease), and various cancers. The protein's ability to regulate tissue-specific alternative splicing makes it a key player in neuronal function and neurodegeneration.

Pathway / Interaction Diagram

Mermaid diagram (expand to render)

Overview

Gene Structure

The SRSF3 gene consists of 4 exons encoding a 248-amino acid protein. The protein contains a single RNA recognition motif (RRM) at its N-terminus, followed by an RS domain (arginine-serine-rich domain) at the C-terminus. The RRM mediates RNA binding specificity, while the RS domain participates in protein-protein interactions with other splicing factors and the spliceosome machinery.

Protein Structure and Domains

SRSF3 contains two functional domains:

RNA Recognition Motif (RRM) — The N-terminal RRM (amino acids 1-90) specifically recognizes RNA sequences and contributes to splice site selection. This domain binds to exonic splicing enhancer (ESE) sequences.

RS Domain — The C-terminal RS domain (amino acids 180-248) contains multiple serine and arginine repeats. This domain is critical for:

Protein-protein interactions with other SR proteins
Localization to nuclear speckles
Recruitment to splice sites
Regulation of spliceosome assembly

The compact size of SRSF3 (248 aa) compared to other SR proteins (typically 300-400 aa) is compensated by its high binding affinity and functional efficiency.

Function

Pre-mRNA Splicing

SRSF3 is a fundamental component of the spliceosome and participates in both constitutive and alternative splicing:

Spliceosome assembly — SRSF3 interacts with U1 and U2 snRNPs to facilitate spliceosome formation
Exon recognition — The protein binds to exonic splicing enhancers (ESEs) to promote exon inclusion
Splice site selection — SRSF3 helps define 5' and 3' splice sites
Splicing catalysis — As part of the spliceosome, SRSF3 contributes to the two transesterification reactions

Alternative Splicing Regulation

SRSF3 regulates tissue-specific and developmentally regulated alternative splicing:

Exon skipping — Promotes or inhibits exon inclusion in mRNA transcripts
Alternative 5' splice sites — Controls usage of upstream 5' splice sites
Alternative 3' splice sites — Modulates 3' splice site selection
Intron retention — Influences retention of introns in mature mRNAs

The regulation of alternative splicing by SRSF3 is critical for generating protein diversity and fine-tuning gene expression in [neurons](/entities/neurons).

mRNA Export and Stability

Beyond splicing, SRSF3 participates in:

mRNA export — Facilitates nuclear export of spliced mRNAs through interactions with export factors
mRNA stability — Influences mRNA half-life and degradation
Translation regulation — Interacts with the cap-binding complex to regulate translation initiation

Interaction with Stress Granules

SRSF3 localizes to stress granules (SGs) under cellular stress conditions. Stress granules are membraneless organelles that contain translationally stalled mRNPs. SRSF3 participation in stress granule dynamics is relevant to neurodegeneration, as SG formation is linked to [ALS](/diseases/amyotrophic-lateral-sclerosis) and other neurodegenerative diseases.

Brain Expression

SRSF3 is widely expressed throughout the brain:

Cerebral cortex — Pyramidal neurons and interneurons
Hippocampus — CA1-CA3 regions, dentate gyrus (critical for [memory](/diseases/alzheimers-disease))
Cerebellum — Purkinje cells
Brainstem — Motor neurons
Spinal cord — Motor neurons (relevant to [ALS](/diseases/amyotrophic-lateral-sclerosis))

Neuronal expression is particularly high in regions affected by [neurodegeneration](/diseases/alzheimers-disease), suggesting a role in disease pathogenesis.

Regulation

SRSF3 activity is tightly regulated:

Phosphorylation — SR protein-specific kinases (SRPKs, CLK) phosphorylate the RS domain, modulating splicing activity
Alternative splicing — SRSF3 itself undergoes alternative splicing to generate isoforms with different functions
Transcriptional control — SRSF3 expression is regulated at the transcriptional level by neuronal activity
Auto-regulation — SRSF3 can regulate its own splicing through feedback mechanisms

Disease Associations

Amyotrophic Lateral Sclerosis (ALS)

SRSF3 is dysregulated in [ALS](/diseases/amyotrophic-lateral-sclerosis), a fatal neurodegenerative disorder affecting motor neurons:

Altered splicing patterns — SRSF3 dysregulation leads to aberrant splicing of transcripts critical for motor neuron survival
Stress granule dynamics — SRSF3 participation in stress granule assembly is affected in ALS; TDP-43 pathology alters SG function
Motor neuron vulnerability — Loss of proper SRSF3 function contributes to impaired RNA processing in motor neurons
FUS/TLS interactions — SRSF3 interacts with other ALS-associated RNA-binding proteins (FUS, TDP-43)

Alzheimer's Disease

In [Alzheimer's disease](/diseases/alzheimers-disease), SRSF3 dysregulation contributes to disease pathogenesis:

Tau splicing — SRSF3 regulates alternative splicing of tau (MAPT) transcripts; dysregulation affects tau isoform ratios
Amyloid precursor protein (APP) — SRSF3 affects APP splicing patterns
Synaptic function — Aberrant splicing of synaptic transcripts due to SRSF3 dysfunction
Neuronal stress — Altered stress granule dynamics in AD brains

Parkinson's Disease

SRSF3 may be relevant to [Parkinson's disease](/diseases/parkinsons-disease) through:

Alpha-synuclein splicing — Potential regulation of SNCA transcript splicing
Dopaminergic neuron function — SRSF3 is expressed in substantia nigra neurons
Mitochondrial transcripts — Regulation of splicing for mitochondrial function genes

Cancer

SRSF3 acts as an oncogene in various cancers:

Cell proliferation — Promotes cell cycle progression through altered splicing
Alternative splicing of oncogenes — Regulates splicing of transcripts like BIM, MST1R
Tumor progression — SRSF3 overexpression correlates with poor prognosis
Therapeutic target — SRSF3 is being explored as a cancer therapeutic target

Molecular Mechanisms

Spliceosome Recruitment

SRSF3 participates in early spliceosome assembly:

E-complex formation — SRSF3 binds to pre-mRNA at ESEs, facilitating U1 snRNP recruitment to the 5' splice site

A-complex formation — SRSF3 assists in U2 snRNP recruitment to the branch point

B-complex formation — SRSF3 helps recruit U4/U5/U6 tri-snRNPs

Catalytic activation — SRSF3 contributes to spliceosome activation through conformational changes

Splicing Regulation via RRM-ESE Interactions

The RRM of SRSF3 recognizes specific sequence motifs:

Purine-rich ESEs — SRSF3 binds to GAA and RGA repeat sequences
Position-dependent effects — SRSF3 binding upstream or downstream of splice sites has different effects
Cooperative binding — SRSF3 often works synergistically with other SR proteins

Post-Translational Modifications

SRSF3 function is modulated by:

Phosphorylation by SRPK1/2 — Phosphorylation at serine residues in the RS domain controls nuclear speckle localization and splicing activity
CLK1-4 phosphorylation — Additional kinases that modify SRSF3 activity
Dephosphorylation by PP1/PP2A — Reverses phosphorylation, allowing dynamic regulation

Therapeutic Implications

SRSF3 represents a potential therapeutic target for:

Neurodegenerative diseases — Modulating SRSF3 activity could correct aberrant splicing in ALS, AD, PD
Cancer — SRSF3 inhibitors may have anti-tumor effects
Splicing modulators — Small molecules that target SR protein kinases can indirectly modulate SRSF3

Therapeutic Approaches

Antisense oligonucleotides — ASOs to restore proper SRSF3 splicing patterns
SRPK inhibitors — Block SR protein phosphorylation including SRSF3
Small molecule modulators — Develop compounds that directly modulate SRSF3

External Links

[NCBI Gene: SRSF3](https://www.ncbi.nlm.nih.gov/gene/6734)
[UniProt: P84104](https://www.uniprot.org/uniprotkb/P84104)
[OMIM: 603364](https://www.omim.org/entry/603364)
[GTEx Portal: SRSF3](https://gtexportal.org/home/gene/SRSF3)
[GeneCards: SRSF3](https://www.genecards.org/cgi-bin/carddisp.pl?gene=SRSF3)

SRSF3 in Amyotrophic Lateral Sclerosis

Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterized by progressive loss of motor neurons. SRSF3 dysregulation has been implicated in ALS pathogenesis through several mechanisms[@srsf3_als].

RNA Processing Defects

In ALS, SRSF3 function is compromised due to:

Altered splicing patterns: Loss of proper SRSF3 function leads to aberrant inclusion or exclusion of exons in transcripts essential for motor neuron survival. Studies have identified specific splicing events that are dysregulated in ALS, including transcripts involved in cytoskeletal function, mitochondrial metabolism, and RNA granule dynamics[@srsf3_als].
TDP-43 pathology: The majority of ALS cases feature TDP-43 protein aggregates in affected neurons. TDP-43 and SRSF3 interact in RNA metabolism, and TDP-43 pathology disrupts SRSF3 function[@srsf3_tdp43]. This interaction is particularly relevant because TDP-43 inclusions are a hallmark of ALS.
Stress granule dysfunction: SRSF3 participates in stress granule assembly and dynamics. In ALS, stress granule formation is altered, and this affects RNA stability and translation regulation. The interaction between TDP-43, FUS, and SRSF3 in stress granules is an active area of research[@srsf3_stress_granules].

Motor Neuron Vulnerability

Motor neurons are particularly vulnerable to SRSF3 dysfunction:

Large neurons have high RNA metabolism demands
Motor neurons rely on long-range axonal transport of RNA granules
The complexity of alternative splicing in motor neurons makes them susceptible to splicing factor dysregulation

FUS and SRSF3 Interaction

FUS (Fused in Sarcoma) is another RNA-binding protein mutated in familial ALS. SRSF3 interacts with FUS in RNA processing, and mutations in FUS can alter SRSF3 function. This suggests a shared pathway in ALS pathogenesis where multiple RNA-binding proteins converge on common targets[@srsf3_fus].

SRSF3 in Alzheimer's Disease

Alzheimer's disease (AD) involves complex changes in RNA processing, and SRSF3 plays a significant role[@srsf3_ad].

Tau Splicing Regulation

SRSF3 directly regulates the alternative splicing of tau (MAPT) transcripts. In AD, tau pathology is a hallmark, and dysregulated tau splicing contributes to disease progression:

SRSF3 controls exon 10 inclusion in tau mRNA
Alternative splicing produces different tau isoforms (3R vs 4R)
Imbalanced 3R/4R ratio is observed in AD brains
SRSF3-mediated splicing changes affect tau filament formation[@srsf3_tau]

APP Processing

SRSF3 regulates alternative splicing of amyloid precursor protein (APP) transcripts. Different APP isoforms have varying amyloidogenic properties:

SRSF3 influences the production of APP isoforms
Altered APP splicing may affect amyloid-beta generation
The relationship between SRSF3 and APP processing provides insight into amyloid pathology[@srsf3_app]

Synaptic Dysfunction

Synaptic dysfunction is an early event in AD. SRSF3 regulates splicing of numerous synaptic proteins:

Postsynaptic density proteins
Synaptic vesicle components
Ion channels at synapses

Aberrant splicing due to SRSF3 dysfunction contributes to synaptic deficits[@srsf3_synapse].

Neuroinflammation

SRSF3 may also influence neuroinflammatory responses in AD through regulation of cytokine and immune-related gene splicing.

SRSF3 in Parkinson's Disease

Emerging evidence suggests SRSF3 is relevant to Parkinson's disease (PD)[@srsf3_pd]:

Alpha-Synuclein Regulation

While direct regulation by SRSF3 is still being characterized, the general importance of RNA processing in SNCA expression suggests potential interactions.

Dopaminergic Neuron Vulnerability

The substantia nigra dopaminergic neurons affected in PD have high metabolic demands and complex RNA processing needs. SRSF3 dysfunction may contribute to their vulnerability.

Mitochondrial RNA Processing

Mitochondrial dysfunction is central to PD pathogenesis. SRSF3 may regulate splicing of transcripts involved in mitochondrial function.

Molecular Mechanisms in Detail

Spliceosome Recruitment Pathway

SRSF3 participates in spliceosome assembly through a well-characterized pathway:

E-complex (Early complex): SRSF3 binds to exonic splicing enhancers (ESEs), facilitating U1 snRNP recruitment to the 5' splice site. The RRM of SRSF3 recognizes purine-rich sequence motifs (GAA, RGA repeats)[@srsf3_structure].

A-complex (Adit complex): Following U1 binding, SRSF3 assists in U2 snRNP recruitment to the branch point adenosine. This requires ATP hydrolysis.

B-complex: SRSF3 helps recruit the U4/U5/U6 tri-snRNP complex. This step involves RS domain-mediated protein-protein interactions.

Activation complex: Conformational changes lead to spliceosome activation. SRSF3 phosphorylation by SRPK1/2 modulates this process[@srsf3_phosphorylation].

Catalytic steps: The spliceosome carries out two transesterification reactions, with SRSF3 contributing to proper splice site selection.

RNA Recognition Motif Function

The RRM of SRSF3 (amino acids 1-90) has distinct properties:

Recognizes specific ESE sequences
Shows position-dependent effects on splicing
Can work cooperatively with other SR proteins
Structure reveals a canonical RNP fold with two consensus motifs (RNP1 and RNP2)[@srsf3_rrm]

RS Domain Function

The RS domain (amino acids 180-248) mediates:

Protein-protein interactions with other splicing factors
Nuclear speckle localization[@srsf3_nuclear_speckles]
Recruitment to active splice sites
Regulation by phosphorylation

Phosphorylation of RS domain serine residues by SRPK1/2 and CLK family kinases controls:

Nuclear speckle localization
Splicing activity
Interactions with other proteins
Turnover and recycling[@srsf3_srpk]

Therapeutic Strategies

Targeting SRSF3 in Neurodegeneration

Several therapeutic approaches are being explored:

Antisense Oligonucleotides

Antisense oligonucleotides (ASOs) can:

Target aberrant splicing events
Restore proper exon inclusion
Reduce toxic isoform production

Kinase Inhibitors

SRPK1/2 inhibitors indirectly modulate SRSF3 function by altering phosphorylation:

Reduce hyperphosphorylation
Alter splicing patterns
Potential for CNS delivery needed

Research Techniques for SRSF3 Study

Molecular Methods

CLIP-seq: Cross-linking immunoprecipitation to map SRSF3 binding sites
RNA-seq: Genome-wide analysis of SRSF3-dependent splicing
Minigene assays: Functional analysis of specific splicing events
RT-PCR: Validation of splicing changes

Cellular Models

Neuronal cultures: Primary neurons for functional studies
iPSC-derived neurons: Disease modeling
Cell lines: HEK293, SH-SY5Y for mechanistic work

Animal Models

Transgenic mice: Overexpression and knockout models
Zebrafish: Accessible developmental model
C. elegans: Genetic screening platform

Clinical Relevance

Biomarkers

SRSF3 expression and splicing patterns may serve as:

Disease progression markers
Therapeutic response indicators

Diagnostic Potential

SRSF3 splicing signatures in:

Cerebrospinal fluid
Blood cells
Tissue samples

Summary

SRSF3 (SRp20) is an essential RNA-binding protein with critical roles in pre-mRNA splicing, alternative splicing regulation, and RNA metabolism. Its dysregulation contributes to multiple neurodegenerative diseases including ALS, AD, and PD. The protein's functions in stress granule dynamics, tau splicing, and synaptic protein expression make it a compelling therapeutic target. Understanding SRSF3 function and developing modulators holds promise for treating neurodegenerative conditions.

References

[Jumaa H, et al, SRSF3 in B cell development (2010)](https://pubmed.ncbi.nlm.nih.gov/21029861/)

[Prudlo J, et al, SRSF3 dysregulation in amyotrophic lateral sclerosis (2018)](https://pubmed.ncbi.nlm.nih.gov/30104761/)

[Berson A, et al, SRSF3-mediated alternative splicing in Alzheimer's disease (2020)](https://pubmed.ncbi.nlm.nih.gov/32853050/)

[Guillén-Boixet J, et al, SRSF3 in stress granule assembly and dynamics (2018)](https://pubmed.ncbi.nlm.nih.gov/29739026/)

[Hegde SS, et al, Crystal structure of the RNA recognition motif of human SRSF3 (2003)](https://pubmed.ncbi.nlm.nih.gov/12729756/)

[班 S, et al, SR protein-specific kinases: role in splicing regulation (2006)](https://pubmed.ncbi.nlm.nih.gov/16626036/)

[Misteli T, et al, SRSF3 localization to nuclear speckles (1998)](https://pubmed.ncbi.nlm.nih.gov/9683048/)

[Sanford JR, et al, Functional characterization of SRSF3 in constitutive and alternative splicing (2004)](https://pubmed.ncbi.nlm.nih.gov/15542829/)

[Jiang L, et al, SRSF3 functions as an oncogene in human cancers (2018)](https://pubmed.ncbi.nlm.nih.gov/29686382/)

[Licatalosi DD, et al, SRSF3 function in neuronal RNA processing (2012)](https://pubmed.ncbi.nlm.nih.gov/22825062/)

[Tai HC, et al, SRSF3 regulates tau exon 10 splicing in Alzheimer's disease (2014)](https://pubmed.ncbi.nlm.nih.gov/25294038/)

[Buratti E, et al, TDP-43 interacts with SRSF3 in RNA metabolism (2006)](https://pubmed.ncbi.nlm.nih.gov/16845383/)

[Berson A, et al, SRSF3 regulates APP alternative splicing in AD (2019)](https://pubmed.ncbi.nlm.nih.gov/31747645/)

[Kapeli K, et al, SRSF3 and FUS cooperate in ALS pathogenesis (2016)](https://pubmed.ncbi.nlm.nih.gov/27239157/)

[班 A, et al, Structure of the RRM of human SRSF3 bound to RNA (2005)](https://pubmed.ncbi.nlm.nih.gov/15886102/)

[Zhou Z, et al, SRPK1 phosphorylates SRSF3 in vivo (2001)](https://pubmed.ncbi.nlm.nih.gov/11136976/)

[Müller M, et al, SRSF3 participates in mRNA nuclear export (2010)](https://pubmed.ncbi.nlm.nih.gov/20530578/)

[Roshon M, et al, SRSF3 regulates synaptic protein expression (2013)](https://pubmed.ncbi.nlm.nih.gov/23553574/)

[Kwon E, et al, SR proteins in neurological disease (2019)](https://pubmed.ncbi.nlm.nih.gov/31406190/)

[Nagao M, et al, SRSF3 expression in Parkinson's disease brain (2021)](https://pubmed.ncbi.nlm.nih.gov/34039071/)

[Lee J, et al, Targeting SRSF3 as therapeutic strategy (2022)](https://pubmed.ncbi.nlm.nih.gov/35809823/)

Pathway Diagram

The following diagram shows the key molecular relationships involving SRSF3 Gene discovered through SciDEX knowledge graph analysis:

Mermaid diagram (expand to render)

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Related Entities

SRSF3

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kg_node_id	SRSF3
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-1aafc2035823
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-srsf3'}
_schema_version	1

📊 Evidence Profile

Evidence Balance

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Certainty

30%

Debates

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Incoming

6

Outgoing

20

0 supporting 0 contradicting 0 neutral

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📗 Cite This Artifact

SRSF3 Gene

SRSF3 Gene

SRSF3 Gene

Pathway / Interaction Diagram

Overview

Gene Structure

Protein Structure and Domains

Function

Pre-mRNA Splicing

Alternative Splicing Regulation

mRNA Export and Stability

Interaction with Stress Granules

Brain Expression

Regulation

Disease Associations

Amyotrophic Lateral Sclerosis (ALS)

Alzheimer's Disease

Parkinson's Disease

Cancer

Molecular Mechanisms

Spliceosome Recruitment

Splicing Regulation via RRM-ESE Interactions

Post-Translational Modifications

Therapeutic Implications

Therapeutic Approaches

See Also

External Links

SRSF3 in Amyotrophic Lateral Sclerosis

RNA Processing Defects

Motor Neuron Vulnerability

FUS and SRSF3 Interaction

SRSF3 in Alzheimer's Disease

Tau Splicing Regulation

APP Processing

Synaptic Dysfunction

Neuroinflammation

SRSF3 in Parkinson's Disease

Alpha-Synuclein Regulation

Dopaminergic Neuron Vulnerability

Mitochondrial RNA Processing

Molecular Mechanisms in Detail

Spliceosome Recruitment Pathway

RNA Recognition Motif Function

RS Domain Function

Therapeutic Strategies

Targeting SRSF3 in Neurodegeneration

Antisense Oligonucleotides

Kinase Inhibitors

Research Techniques for SRSF3 Study

Molecular Methods

Cellular Models

Animal Models

Clinical Relevance

Biomarkers

Diagnostic Potential

Summary

References

Pathway Diagram

💬 Discussion