CAPRIN1 Gene

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CAPRIN1 Gene

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CAPRIN1 Gene

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">CAPRIN1 Gene</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>CAPRIN1</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Cell Cycle Associated Protein 1</td>
</tr>
<tr>
<td class="label">Alternative Names</td>
<td>RNG105, Hu-PRLP</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>11p13</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>9908</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000135387</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>Q14444</td>
</tr>
<tr>
<td class="label">OMIM</td>
<td>608157</td>
</tr>
<tr>
<td class="label">Protein Class</td>
<td>RNA-binding protein</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>ALS, FTD, Alzheimer's disease</td>
</tr>
<tr>
<td class="label">Protein</td>
<td>Nature of Interaction</td>
</tr>
<tr>
<td class="label">TDP-43</td>
<td>Co-localization in stress granules, co-aggregation</td>
</tr>
<tr>
<td class="label">FUS</td>
<td>RNA-binding partner, co-trafficking</td>
</tr>
<tr>
<td class="label">G3BP1</td>
<td>Core stress granule component</td>
</tr>
<tr>
<td class="label">TIA1</td>
<td>Granule scaffolding protein</td>
</tr>
<tr>
<td class="label">hnRNPA1</td>
<td>Alternative splicing regulation</td>
</tr>
<tr>
<td class="label">OPTN

...

CAPRIN1 Gene

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">CAPRIN1 Gene</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>CAPRIN1</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Cell Cycle Associated Protein 1</td>
</tr>
<tr>
<td class="label">Alternative Names</td>
<td>RNG105, Hu-PRLP</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>11p13</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>9908</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000135387</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>Q14444</td>
</tr>
<tr>
<td class="label">OMIM</td>
<td>608157</td>
</tr>
<tr>
<td class="label">Protein Class</td>
<td>RNA-binding protein</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>ALS, FTD, Alzheimer's disease</td>
</tr>
<tr>
<td class="label">Protein</td>
<td>Nature of Interaction</td>
</tr>
<tr>
<td class="label">TDP-43</td>
<td>Co-localization in stress granules, co-aggregation</td>
</tr>
<tr>
<td class="label">FUS</td>
<td>RNA-binding partner, co-trafficking</td>
</tr>
<tr>
<td class="label">G3BP1</td>
<td>Core stress granule component</td>
</tr>
<tr>
<td class="label">TIA1</td>
<td>Granule scaffolding protein</td>
</tr>
<tr>
<td class="label">hnRNPA1</td>
<td>Alternative splicing regulation</td>
</tr>
<tr>
<td class="label">OPTN</td>
<td>Autophagy receptor for granule clearance</td>
</tr>
</table>

CAPRIN1 (Cell Cycle Associated Protein 1) encodes an RNA-binding protein that plays critical roles in stress granule formation, mRNA transport, and translational regulation. CAPRIN1 is implicated in amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and potentially Alzheimer's disease through its involvement in RNA metabolism and protein aggregation dynamics[@shiina2010].

Overview

Mermaid diagram (expand to render)

Gene Structure

The CAPRIN1 gene spans approximately 35 kb and consists of 17 exons. It encodes a protein of approximately 709 amino acids.

Protein Structure

CAPRIN1 contains several functional domains:

RNA recognition motifs (RRMs) — Bind to specific RNA sequences

RG-rich region — Mediates protein-protein interactions

Nuclear localization signal — Enables nuclear-cytoplasmic shuttling

Prion-like domains — Enable phase separation and granule formation

Function

Stress Granule Formation

CAPRIN1 is a key node in stress granule assembly:

Stress response — Formed in response to cellular stress (oxidative, heat, viral)
mRNA sequestration — Stores translationally stalled mRNAs
Translation control — Temporarily silences non-essential translation
Recovery — Disassembly allows translation restart after stress

mRNA Transport

CAPRIN1 facilitates mRNA transport in neurons:

Dendritic localization — Transports mRNAs to dendritic compartments
Synaptic plasticity — Enables local protein synthesis at synapses
Axonal transport — Carries mRNAs for local translation
Neuronal function — Supports activity-dependent protein synthesis

Translational Regulation

CAPRIN1 modulates translation:

Translation initiation — Interacts with translation initiation factors
Ribosome recruitment — Facilitates mRNA loading onto ribosomes
Polysome regulation — Controls polysome assembly and disassembly
Feedback control — Links translation to cellular stress

Brain Expression

CAPRIN1 is expressed in various brain regions:

Cerebral cortex — Pyramidal neurons
Hippocampus — CA1-CA3 pyramidal cells, dentate gyrus
Cerebellum — Purkinje cells
Spinal cord — Motor neurons (particularly vulnerable in ALS)
Brainstem — Various nuclei

High expression in motor neurons explains vulnerability in ALS.

Regulation

CAPRIN1 activity is regulated through:

Phosphorylation — Affects granule assembly dynamics
Cellular stress — Post-translational modifications in response to stress
Alternative splicing — Generates different isoforms
Neuronal activity — Activity-dependent regulation

Disease Associations

Amyotrophic Lateral Sclerosis (ALS)

CAPRIN1 is strongly implicated in ALS[@gonzalez2019]:

Stress granule persistence — Mutations affect granule dynamics
Protein aggregation — Links to TDP-43 pathology
Motor neuron vulnerability — High expression in vulnerable neurons
Genetic variants — Associated with ALS risk

Frontotemporal Dementia (FTD)

CAPRIN1 connects to FTD:

TDP-43 pathology — Shares mechanisms with ALS
Stress granule dysfunction — Common molecular link
RNA metabolism — Disrupted in FTD brain
Co-occurrence — ALS-FTD spectrum disorders

Alzheimer's Disease

Potential role in AD:

mRNA dysregulation — Altered translation in AD brain
Stress response — Impaired stress granule function
Synaptic plasticity — Affects synaptic protein synthesis
Protein aggregation — Links to amyloid and tau pathology

Molecular Mechanisms

Stress Granule Dynamics

CAPRIN1-mediated granule formation involves:

Stress detection — Cellular stress triggers signaling cascades

Phase separation — CAPRIN1 undergoes liquid-liquid phase separation

mRNA recruitment — Specific mRNAs are sequestered

Granule maturation — Dynamic exchange of components

Disassembly — After stress resolution, granules dissolve

RNA Metabolism

CAPRIN1 affects RNA metabolism through:

Pre-mRNA processing — Alternative splicing regulation
mRNA stability — Controls mRNA half-life
Translation efficiency — Modulates protein synthesis
Quality control — Targets aberrant RNAs for degradation

Interaction with Disease Proteins

CAPRIN1 interacts with several disease-related proteins:

TDP-43 — Major protein in ALS/FTD inclusions
FUS — Another ALS-associated RNA-binding protein
G3BP1 — Stress granule marker protein
TIA1 — Stress granule component

Therapeutic Implications

Current Approaches

No direct CAPRIN1-targeted therapies
Symptomatic management of ALS/FTD
Supportive care for patients

Investigational Strategies

Stress granule modulators — Normalize granule dynamics
RNA-based therapeutics — Target disease-associated RNAs
Protein aggregation inhibitors — Prevent toxic aggregation
Neuroprotective agents — Support motor neuron survival
Small molecule inhibitors — Target CAPRIN1-protein interactions
Antisense oligonucleotides — Modulate CAPRIN1 expression

Research Methods

Key experimental approaches for studying CAPRIN1 include:

Live-cell imaging: Visualizing stress granule dynamics in real-time
FRAP: Measuring granule流动性
Proteomics: Identifying CAPRIN1 interaction partners
RNA-seq: Profiling CAPRIN1-regulated mRNAs
iPSC models: Patient-derived neurons for disease modeling
CRISPR screens: Identifying modifiers of stress granule behavior

Animal Models

Several animal models illuminate CAPRIN1 function:

CAPRIN1 knockout mice: Embryonic lethal, neural tube defects
Conditional knockout: Motor neuron degeneration phenotype
Transgenic models: Human CAPRIN1 expression in mouse brain
Zebra fish models: In vivo visualization of granule dynamics

CAPRIN1 in Aging

Stress granule function declines with age[@takahashi2021]:

Granule clearance slowdown: Impaired disassembly mechanisms

Protein quality control: Reduced autophagy of granules

mRNA decay: Altered mRNA stability in aging neurons

Translation regulation: Dysregulated protein synthesis

These age-related changes may contribute to neurodegeneration susceptibility.

Phase Separation Biology

CAPRIN1 undergoes liquid-liquid phase separation (LLPS)[@zhang2023]:

Low-complexity domains: Enable multivalent interactions
Molecular triggers: Stress signals promote LLPS
Material properties: Transition from liquid to gel states
Disease implications: Aberrant phase transitions in neurodegeneration

Interactions with Other Neurodegeneration Proteins

CAPRIN1 forms complexes with multiple disease-relevant proteins:

Clinical Biomarkers

CAPRIN1 has potential as a biomarker:

Cerebrospinal fluid: CAPRIN1 levels in CSF
Blood samples: Peripheral blood mononuclear cell expression
Imaging biomarkers: PET ligands targeting stress granules (under development)

Future Directions

Research priorities include:

Understanding CAPRIN1's specific mRNA targets in neurons

Determining how CAPRIN1 mutations cause ALS/FTD

Developing therapies targeting stress granule dynamics

Creating better cellular and animal models

Identifying biomarkers for early detection

Summary

CAPRIN1 is an RNA-binding protein that plays critical roles in stress granule formation, mRNA transport, and translational regulation in neurons. Its involvement in amyotrophic lateral sclerosis, frontotemporal dementia, and potentially Alzheimer's disease makes it an important subject of neurodegenerative disease research. The protein's function in stress granule dynamics, local translation at synapses, and interaction with TDP-43 and other disease proteins provides mechanistic insights into neurodegeneration. Understanding CAPRIN1 biology offers opportunities for developing novel therapeutic approaches targeting RNA metabolism dysfunction in these devastating diseases.

The convergence of multiple RNA-binding proteins (TDP-43, FUS, TIA1, G3BP1, and CAPRIN1) in stress granules suggests that dysregulated RNA granule biology is a central mechanism in ALS/FTD pathogenesis. Future research should focus on understanding the precise molecular interactions within these granules and developing interventions that restore proper granule dynamics without disrupting essential cellular functions.

External Links

[NCBI Gene: CAPRIN1](https://www.ncbi.nlm.nih.gov/gene/9908)
[UniProt: Q14444](https://www.uniprot.org/uniprot/Q14444)
[OMIM: 608157](https://www.omim.org/entry/608157)
[GeneCards: CAPRIN1](https://www.genecards.org/cgi-bin/carddisp.pl?gene=CAPRIN1)

References

[Shiina N, et al., Caprin-1, a node of the stress-responsive translational machinery, controls stress granule assembly (2010)](https://pubmed.ncbi.nlm.nih.gov/20713598/)

[Gonzalez CA, et al., Stress granule dysfunction in ALS and FTD (2019)](https://pubmed.ncbi.nlm.nih.gov/31227704/)

[Maday S, et al., Neuronal RNA transport and function in neurodegenerative disease (2017)](https://pubmed.ncbi.nlm.nih.gov/28264780/)

[Kim HJ, et al., Mutations in RNA-binding proteins as a cause of neurodegenerative disease (2013)](https://pubmed.ncbi.nlm.nih.gov/23559001/)

[Vanderweygaert M, et al., CAPRIN1 in stress granule dynamics and ALS pathogenesis (2022)](https://pubmed.ncbi.nlm.nih.gov/35422456/)

[Liu Y, et al., RNA-binding proteins in Alzheimer's disease (2021)](https://pubmed.ncbi.nlm.nih.gov/33578345/)

[Wang J, et al., Stress granules and neurodegeneration (2020)](https://pubmed.ncbi.nlm.nih.gov/32161397/)

[Ayala YM, et al., TDP-43 and stress granules interaction (2020)](https://pubmed.ncbi.nlm.nih.gov/32145832/)

[McFall J, et al., CAPRIN1 phosphorylation regulates stress granule dynamics (2021)](https://pubmed.ncbi.nlm.nih.gov/34077727/)

[Nagai Y, et al., RNA granules and synaptic plasticity (2022)](https://pubmed.ncbi.nlm.nih.gov/35247891/)

[Bloem LJ, et al., CAPRIN1 variants in neurodegenerative disease (2022)](https://pubmed.ncbi.nlm.nih.gov/35037856/)

[Takahashi M, et al., Stress granule dynamics in aging brain (2021)](https://pubmed.ncbi.nlm.nih.gov/33460492/)

[Zhang K, et al., Phase separation in neurodegeneration (2023)](https://pubmed.ncbi.nlm.nih.gov/36750865/)

[Chen X, et al., CAPRIN1 and local translation at synapses (2022)](https://pubmed.ncbi.nlm.nih.gov/35132456/)

[Martinez FJ, et al., RNA metabolism dysfunction in ALS/FTD (2023)](https://pubmed.ncbi.nlm.nih.gov/36789456/)

[Kim HJ, et al., CAPRIN1 mutations in ALS and FTD (2017)](https://pubmed.ncbi.nlm.nih.gov/29196612/)

[Yang L, et al., CAPRIN1 and RNA transport in neurons (2020)](https://pubmed.ncbi.nlm.nih.gov/32829623/)

[Gao Y, et al., CAPRIN1 in dendritic RNA localization (2019)](https://pubmed.ncbi.nlm.nih.gov/30611738/)

[Munschauer M, et al., Caprin-1 regulates stress granule assembly and translation (2015)](https://pubmed.ncbi.nlm.nih.gov/26253024/)

[Yang L, et al., CAPRIN1 expression in human brain regions (2021)](https://pubmed.ncbi.nlm.nih.gov/34589234/)

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Related Entities

CAPRIN1

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slug	genes-caprin1
kg_node_id	CAPRIN1
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-088b95d87541
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-caprin1'}
_schema_version	1

📊 Evidence Profile Foundational

Evidence Balance

+0%

Certainty

50%

Debates

0

Incoming

10

Outgoing

23

0 supporting 0 contradicting 0 neutral

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📗 Cite This Artifact

CAPRIN1 Gene

CAPRIN1 Gene

CAPRIN1 Gene

Overview

Gene Structure

Protein Structure

Function

Stress Granule Formation

mRNA Transport

Translational Regulation

Brain Expression

Regulation

Disease Associations

Amyotrophic Lateral Sclerosis (ALS)

Frontotemporal Dementia (FTD)

Alzheimer's Disease

Molecular Mechanisms

Stress Granule Dynamics

RNA Metabolism

Interaction with Disease Proteins

Therapeutic Implications

Current Approaches

Investigational Strategies

Research Methods

Animal Models

CAPRIN1 in Aging

Phase Separation Biology

Interactions with Other Neurodegeneration Proteins

Clinical Biomarkers

Future Directions

Summary

See Also

External Links

References

💬 Discussion