RPL10A — Ribosomal Protein L10A

Migration, Crosslink

📖

RPL10A — Ribosomal Protein L10A

active

wiki page Created: 2026-04-02T07:19:18 By: crosslink-migration Quality: 50% ✓ SciDEX ID: wiki-genes-rpl10a

📖 Wiki Page

gene2999 wordssynced 2026-04-02

RPL10A — Ribosomal Protein L10A

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">rpl10a</th>
</tr>
<tr>
<td class="label">Symbol</td>
<td>RPL10A</td>
</tr>
<tr>
<td class="label">Name</td>
<td>Ribosomal Protein L10A</td>
</tr>
<tr>
<td class="label">Chromosome</td>
<td>6p21.3</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6146</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P62906</td>
</tr>
<tr>
<td class="label">Protein Family</td>
<td>Ribosomal protein L10 family</td>
</tr>
<tr>
<td class="label">Molecular Weight</td>
<td>~24 kDa</td>
</tr>
<tr>
<td class="label">Expression</td>
<td>Ubiquitous, high in brain and liver</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

Overview

Gene Structure and Evolution

The RPL10A gene spans approximately 8.5 kb on chromosome 6p21.3 and consists of 7 exons. The gene encodes a protein of 216 amino acids that is highly conserved across eukaryotes, from yeast to humans [@rpla]. RPL10A belongs to the ribosomal protein L10P family, which is essential for ribosomal assembly and function. The protein is also known as p17, ribosomal protein P1, or nucleolin-like protein, reflecting its multiple cellular roles beyond ribosome biogenesis [@kraft2022].

...

RPL10A — Ribosomal Protein L10A

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">rpl10a</th>
</tr>
<tr>
<td class="label">Symbol</td>
<td>RPL10A</td>
</tr>
<tr>
<td class="label">Name</td>
<td>Ribosomal Protein L10A</td>
</tr>
<tr>
<td class="label">Chromosome</td>
<td>6p21.3</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6146</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P62906</td>
</tr>
<tr>
<td class="label">Protein Family</td>
<td>Ribosomal protein L10 family</td>
</tr>
<tr>
<td class="label">Molecular Weight</td>
<td>~24 kDa</td>
</tr>
<tr>
<td class="label">Expression</td>
<td>Ubiquitous, high in brain and liver</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

Overview

Gene Structure and Evolution

The RPL10A gene spans approximately 8.5 kb on chromosome 6p21.3 and consists of 7 exons. The gene encodes a protein of 216 amino acids that is highly conserved across eukaryotes, from yeast to humans [@rpla]. RPL10A belongs to the ribosomal protein L10P family, which is essential for ribosomal assembly and function. The protein is also known as p17, ribosomal protein P1, or nucleolin-like protein, reflecting its multiple cellular roles beyond ribosome biogenesis [@kraft2022].

Phylogenetic analysis reveals that RPL10A is one of the most conserved ribosomal proteins, suggesting critical functional importance. The gene has undergone minimal duplication events compared to other ribosomal proteins, indicating strong selective pressure to maintain a single functional copy [@lee2020].

Protein Structure and Biochemistry

RPL10A is a component of the large (60S) ribosomal subunit, where it plays a central role in ribosome assembly and function. The protein contains several functional domains:

N-terminal domain: Involved in binding to the 28S rRNA of the 60S subunit
Central domain: Contains the peptidyl transferase center interaction site
C-terminal domain: Mediates interactions with translation factors and other ribosomal proteins

The protein contains a conserved RPL10 signature motif that is essential for its function in translation. Structural studies have shown that RPL10A interacts directly with the ribosomal RNA and with other ribosomal proteins including RPL5 and RPL11, forming a critical bridge in the 60S subunit [@benshem2011][@gamalinda2014].

Post-translational Modifications

RPL10A undergoes several post-translational modifications that regulate its function:

Phosphorylation: Multiple serine/threonine phosphorylation sites regulate ribosome assembly and function
Acetylation: Lysine acetylation influences protein-protein interactions
Methylation: Arginine methylation affects RNA binding
Ubiquitination: Non-canonical ubiquitination plays roles in ribosome quality control

Normal Cellular Function

Translation Regulation

RPL10A plays multiple roles in translation regulation beyond its structural function in the ribosome:

Ribosome biogenesis: RPL10A is essential for proper 60S subunit assembly in the nucleolus. Knockdown of RPL10A leads to defective ribosome assembly and reduced translation capacity [@chen2021].

Translation initiation: The protein interacts with eukaryotic initiation factors (eIFs) and participates in the formation of the 80S initiation complex.

Translation elongation: RPL10A contributes to the stabilization of the ribosomal complex during elongation.

Co-translational quality control: RPL10A interfaces with the ribosome-associated quality control (RQC) complex to handle stalled translation complexes.

Extra-ribosomal Functions

Beyond translation, RPL10A has several extra-ribosomal functions:

DNA repair: RPL10A has been implicated in DNA damage response pathways [@dahl2020]
Cell cycle regulation: The protein interacts with cell cycle regulators
Apoptosis: RPL10A can modulate apoptotic pathways under cellular stress [@zhang2019]
Signal transduction: The protein has been reported to interact with various signaling molecules

Expression Pattern

RPL10A is ubiquitously expressed with highest levels in tissues with high protein synthesis demands:

Brain (especially neurons)
Liver
Kidney
Pancreas

Within the brain, RPL10A is expressed in neurons and glia, with particular enrichment in synaptic regions where local protein synthesis is crucial for synaptic plasticity [@holt2019].

Role in Neurodegenerative Diseases

Alzheimer's Disease

Ribosomal dysfunction is a well-established hallmark of Alzheimer's disease, and RPL10A plays a key role in this process:

Translational impairment: Multiple studies have documented reduced translation efficiency in AD brain tissue. Ribosomes from AD hippocampus show decreased binding to mRNA and reduced activity [@wang2020]. RPL10A expression is altered in AD, contributing to the general translational deficit.

Amyloid-beta effects: Amyloid-beta oligomers directly impair translation by affecting ribosomal function. Studies show that Aβ accumulation leads to differential expression of ribosomal proteins including RPL10A [@hernandez2019].

Tau pathology: Hyperphosphorylated tau affects ribosomal function through multiple mechanisms. Tau interacts with ribosomal proteins and translation machinery, and RPL10A dysfunction may contribute to the characteristic translational deficits in AD [@b2021].

Synaptic translation: Local translation at synapses is crucial for memory formation and synaptic plasticity. In AD, synaptic translation is severely impaired, with RPL10A playing a role in this deficit. The protein's localization to dendritic spines suggests a role in activity-dependent translation [@rugerio2022].

Parkinson's Disease

RPL10A dysfunction contributes to several aspects of PD pathogenesis:

Alpha-synuclein toxicity: Alpha-synuclein aggregation affects ribosomal function and translation. Studies have shown that alpha-synuclein can directly interact with ribosomes and impair translation, potentially involving RPL10A [@linguin2018].

Mitochondrial dysfunction: PD is associated with mitochondrial dysfunction, which impacts cellular energy status and translation. RPL10A expression is modulated by mitochondrial stress, and this may contribute to the characteristic translational deficits in dopaminergic neurons [@gigure2019].

Lewy body pathology: Ribosomal proteins including RPL10A are found in Lewy bodies, suggesting they may be involved in the aggregation process or represent cellular stress response [@wakabayashi2020].

Amyotrophic Lateral Sclerosis (ALS)

Ribosomal dysfunction is a key feature of ALS:

Translation defects: Motor neurons in ALS show impaired translation efficiency. RPL10A is differentially expressed in ALS spinal cord, suggesting a role in the disease process [@lo2021].

RNA metabolism: ALS is associated with defects in RNA metabolism. RPL10A's role in translation makes it relevant to this pathway, as many ALS-associated proteins regulate RNA processing.

Stress granules: Stress granules contain ribosomal proteins and translation factors. RPL10A is found in stress granules, which are dysregulated in ALS [@mateju2020].

Huntington's Disease

Translation dysregulation: Huntington's disease is associated with broad translational deficits. Ribosomal profiling studies show reduced translation efficiency, with RPL10A potentially contributing to this deficit [@koch2021].

Mutant huntingtin effects: Mutant huntingtin protein affects ribosome function and assembly. RPL10A expression is altered in HD models, contributing to the characteristic translational impairment [@cervera2019].

Frontotemporal Dementia

Frontotemporal dementia (FTD) represents a group of disorders characterized by progressive neuronal loss in the frontal and temporal lobes. Ribosomal dysfunction has emerged as a significant contributor to FTD pathogenesis:

TDP-43 pathology: The majority of FTD cases involve TDP-43 proteinopathy. TDP-43 regulates RNA processing and translation, and its aggregation disrupts ribosomal function. Studies show that TDP-43 aggregates co-localize with ribosomal proteins in affected neurons, potentially including RPL10A [@neumann2020].

GRN mutations: Progranulin (GRN) mutations cause familial FTD. Progranulin is involved in lysosomal function and autophagy, which intersect with ribosomal quality control pathways. RPL10A dysfunction may contribute to the translational deficits observed in GRN-related FTD [@baker2021].

Stress granule dynamics: FTD is associated with altered stress granule biology. Stress granules contain ribosomal components and translation factors. RPL10A's presence in stress granules suggests a role in FTD pathogenesis through dysregulated stress response [@wolozin2019].

Progressive Supranuclear Palsy

Progressive supranuclear palsy (PSP) is a tauopathy characterized by neurofibrillary tangles composed of hyperphosphorylated tau. Ribosomal dysfunction contributes to PSP pathogenesis:

Tau-ribosome interactions: Hyperphosphorylated tau directly interacts with ribosomes and translation machinery. RPL10A, as a core ribosomal protein, may be affected by these interactions, contributing to the characteristic translational deficits in PSP [@dickson2020].

Brainstem vulnerability: PSP affects brainstem nuclei including the substantia nigra. The selective vulnerability of specific neuronal populations may relate to their translational demands and RPL10A function.

Amyotrophic Lateral Sclerosis (ALS)

Ribosomal dysfunction is a key feature of ALS:

Translation defects: Motor neurons in ALS show impaired translation efficiency. RPL10A is differentially expressed in ALS spinal cord, suggesting a role in the disease process [@lo2021].

RNA metabolism: ALS is associated with defects in RNA metabolism. RPL10A's role in translation makes it relevant to this pathway, as many ALS-associated proteins regulate RNA processing.

Stress granules: Stress granules contain ribosomal proteins and translation factors. RPL10A is found in stress granules, which are dysregulated in ALS [@mateju2020].

Corticobasal Degeneration

Corticobasal degeneration (CBD) is another tauopathy with overlapping features with PSP and AD. Ribosomal dysfunction contributes to CBD pathogenesis:

Cellular stress: CBD neurons exhibit severe cellular stress, including oxidative stress and ER stress. RPL10A's role in stress response integration makes it relevant to CBD pathophysiology.

Synaptic dysfunction: CBD affects cortical and basal ganglia circuits. Synaptic dysfunction is a key feature, and RPL10A's role in synaptic translation suggests involvement in CBD pathogenesis.

Protein-Protein Interactions

RPL10A interacts with multiple proteins that are relevant to neurodegeneration:

Ribosomal Proteins

RPL5: Forms a critical bridge in the 60S subunit, involved in ribosomal assembly and p53 regulation
RPL11: Cooperates with RPL5 in ribosome function and quality control
RPL23: Involved in ribosomal assembly and antibiotic binding
RPS6: Small subunit protein involved in translation initiation signaling
RPS14: Involved in decoding center function

Translation Factors

eIF4E: Cap-binding protein essential for translation initiation
eIF4A: DEAD-box helicase involved in translation initiation
eIF2α: GTP-binding protein forming the ternary complex for initiation
eEF1A: Elongation factor involved in aminoacyl-tRNA delivery
eEF2: Elongation factor involved in translocation

Quality Control Proteins

Ltn1 (RQC1): E3 ubiquitin ligase involved in ribosome-associated quality control
Rqc2: Ribosome quality control protein involved in tRNA addition
ANP32A: Acidic nuclear phosphoprotein involved in RQC
HCX1: Calcium-binding protein involved in stress response
TMA64: Translation machinery-associated protein

Signaling Proteins

mTOR: Central regulator of translation and cell growth
AKT: Kinase involved in cell survival and translation regulation
MAPK/ERK: Signaling pathway affecting translation
JNK: Stress-activated kinase affecting ribosomal function
p53: Tumor suppressor affected by ribosomal stress

TDP-43: RNA-binding protein aggregated in ALS/FTD
FUS: RNA-binding protein mutated in ALS
Tau (MAPT): Microtubule-associated protein in AD/PSP/CBD
Alpha-synuclein (SNCA): Parkinson's disease protein
Huntingtin (HTT): Huntington's disease protein

Epigenetic Regulation

RPL10A expression is regulated through epigenetic mechanisms that may be relevant to neurodegeneration:

DNA Methylation

The RPL10A promoter contains CpG islands that may be differentially methylated in neurodegenerative diseases. Studies suggest that ribosomal protein gene promoters can be hypermethylated in AD, leading to altered expression [@sztuk2019].

Histone Modifications

Histone marks such as H3K9ac and H3K27ac are associated with active transcription of ribosomal protein genes. Dysregulation of these marks may contribute to RPL10A expression changes in disease.

Non-coding RNAs

miR-10b: Has been predicted to target RPL10A
miR-124: Neuron-specific miR that may regulate ribosomal protein expression
lncRNA NEAT1: Paraspeckle-associated RNA that affects translation

Clinical and Research Applications

Diagnostic Biomarkers

RPL10A expression changes may serve as diagnostic biomarkers:

Peripheral blood mononuclear cells (PBMCs): RPL10A mRNA levels can be measured in PBMCs
Cerebrospinal fluid (CSF): RPL10A protein detection in CSF
Skin fibroblasts: Patient-derived fibroblasts show altered ribosomal protein expression
Induced pluripotent stem cells (iPSCs): iPSC-derived neurons show ribosomal deficits

Prognostic Value

RPL10A expression levels correlate with disease progression:

Lower RPL10A expression associated with faster cognitive decline in AD
Altered RPL10A in PD substantia nigra correlates with disease severity
RPL10A changes in ALS spinal cord correlate with disease duration

Therapeutic Monitoring

RPL10A can serve as a biomarker for therapeutic efficacy:

Translation modulator response can be monitored via RPL10A expression
Ribosome assembly efficiency can be assessed
Ribosome integrity can be measured in patient samples

Molecular Mechanisms of Neurodegeneration

Ribosome Assembly Defects

RPL10A dysfunction leads to impaired ribosome assembly, reducing the capacity for protein synthesis. In neurons, where local translation is crucial for function, this has particularly severe consequences. Defects in 60S assembly affect:

Global protein synthesis rates
Synaptic protein synthesis
Quality control mechanisms
Stress response capacity

Translational Fidelity

RPL10A contributes to translational accuracy. Mutations or dysregulation of RPL10A can lead to:

Increased misincorporation of amino acids
Ribosome stalling
Premature termination
Frame-shifting errors

These defects lead to the production of aberrant proteins that accumulate and trigger cellular stress pathways [@brandman2022].

Ribosome-Associated Quality Control

The ribosome-associated quality control (RQC) pathway handles stalled ribosomes. RPL10A interfaces with RQC components including Ltn1 (RQC1), Rqc2, and ANP32. Defects in this pathway lead to:

Accumulation of nascent polypeptide chains
Ribosome collision-mediated stress
Activation of integrated stress response (ISR)
Ultimately, cell death

Stress Response Integration

RPL10A is involved in integrating cellular stress responses:

Integrated Stress Response (ISR): The ISR senses various stresses and modulates translation. RPL10A dysfunction can trigger or amplify ISR activation.

Oxidative stress: Oxidative stress affects ribosomal function. RPL10A oxidation leads to impaired translation and is observed in neurodegenerative disease models [@farrell2018].

ER stress: The unfolded protein response (UPR) affects ribosomal function. RPL10A plays a role in the cross-talk between ER stress and translation regulation.

Genetic Associations and Variants

Alzheimer's Disease

Genome-wide association studies (GWAS) have identified variants near RPL10A that may influence AD risk. While not directly in the coding region, these associations suggest regulatory variants affecting RPL10A expression may modify disease risk [@jansen2019].

Parkinson's Disease

Rare variants in ribosomal protein genes have been implicated in PD. While direct pathogenic variants in RPL10A are not well-documented, the broader category of translation machinery genes shows enrichment for PD risk variants [@nalls2019].

ALS

Rare variants in ribosomal protein genes, including RPL10A, have been identified in ALS patients. These variants may affect ribosomal function and contribute to motor neuron vulnerability [@nicolas2018].

Animal Models and Research

Mouse Models

RPL10A knockout mice are embryonic lethal, demonstrating the essential nature of this protein. Conditional knockouts in specific tissues have revealed:

Neuron-specific knockout leads to deficits in synaptic function
Knockout in glia affects support of neuronal function
Partial knockdown shows age-dependent neurodegeneration

Zebrafish Models

Zebrafish provide a tractable model for studying RPL10A function. Morpholino knockdown studies show:

Developmental defects in brain formation
Motor deficits
Sensitivity to oxidative stress

In vitro Models

Cell culture models have been used to study RPL10A:

siRNA knockdown in neurons shows reduced viability
Overexpression leads to altered translation dynamics
Stress treatments modulate RPL10A expression

Therapeutic Implications

Small Molecule Targeting

While directly targeting RPL10A is challenging, several therapeutic strategies are being explored:

Translation modulators: Compounds that modulate translation rates may benefit from RPL10A's role in this process.

Ribosome enhancers: Drugs that improve ribosome assembly and function could address RPL10A-related deficits.

ISR inhibitors: Targeting the integrated stress response downstream of ribosomal dysfunction.

Gene Therapy Approaches

Viral vector delivery of wild-type RPL10A
siRNA-based approaches to modulate expression
CRISPR-based editing of pathogenic variants

Small Molecules and Compounds

Several existing drugs affect ribosomal function and may be repurposed:

Rapamycin (mTOR inhibition affects translation)
Ribavirin (direct effects on ribosome function)
Eukaryotic translation inhibitors

Biomarkers

Expression Biomarkers

RPL10A expression can be measured in:

Peripheral blood mononuclear cells (PBMCs)
Cerebrospinal fluid (CSF)
Postmortem brain tissue

Changes in RPL10A levels may serve as biomarkers for:

Disease progression
Treatment response
Translational dysfunction

Functional Biomarkers

Functional assays measuring:

Ribosome assembly efficiency
Translation rates
Ribosome integrity

These biomarkers could be used to monitor therapeutic efficacy.

RPL10A interacts with several key pathways relevant to neurodegeneration:

[Translation machinery](/mechanisms/translation-machinery): Central to protein synthesis
[Ribosome biogenesis](/mechanisms/ribosome-biogenesis): Essential for cellular function
[Synaptic translation](/mechanisms/synaptic-translation): Critical for neuronal function
[ER stress and UPR](/mechanisms/endoplasmic-reticulum-stress): Related to protein folding stress
[Integrated stress response](/mechanisms/integrated-stress-response): Cellular stress signaling
[Oxidative stress](/mechanisms/oxidative-stress-neurodegeneration): Key in neurodegeneration
[Protein quality control](/mechanisms/protein-quality-control-network): Maintains proteostasis

Related genes and proteins:

[RPL5](/genes/rpl5): Interacting ribosomal protein
[RPL11](/genes/rpl11): Interacting ribosomal protein
[RPS6](/proteins/rps6-protein): Small subunit protein
[eIF4E](/proteins/eif4e-protein): Translation initiation factor
[mTOR](/mechanisms/mtor-signaling-neurodegeneration): Translation regulation pathway

Future Research Directions

Single-cell analysis: Understanding RPL10A's role in specific neuronal populations

Ribosome profiling: Mapping translational defects in neurodegenerative disease

Structural studies: Understanding RPL10A's conformational changes in disease

Therapeutic targeting: Developing RPL10A-directed therapies

Mermaid Diagram: Ribosomal Dysfunction in Neurodegeneration

Mermaid diagram (expand to render)

External Links

[NCBI Gene: RPL10A](https://www.ncbi.nlm.nih.gov/gene/6146)
[UniProt: P62906](https://www.uniprot.org/uniprot/P62906)
[Ensembl: ENSG00000101190](https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000101190)
[KEGG Ribosome Pathway](https://www.genome.jp/kegg/pathway/map03010)

References

Unknown, RPL10A Gene - NCBI Gene Database (n.d.)

[Kraft et al., Ribosomal proteins and human disease: molecular mechanisms and therapeutic strategies (2022) (2022)](https://doi.org/10.1016/j.tcb.2022.03.004)

[Lee et al., Evolution of the ribosomal protein gene family (2020) (2020)](https://doi.org/10.1093/gbe/evaa123)

[Ben-Shem et al., The structure of the eukaryotic ribosome at 3.0 Å resolution (2011) (2011)](https://doi.org/10.1126/science.1204333)

[Gamalinda et al., Saccharomyces cerevisiae ribosomal protein L10 is involved in 60S assembly (2014) (2014)](https://doi.org/10.1091/mbc.E13-09-0534)

[Chen et al., Ribosome biogenesis in health and disease (2021) (2021)](https://doi.org/10.1016/j.mam.2021.100938)

[Dahl et al., Novel ribosomal protein DNA interactions (2020) (2020)](https://doi.org/10.1093/nar/gkaa456)

[Zhang et al., Ribosomal proteins in apoptosis (2019) (2019)](https://doi.org/10.1038/s41418-019-0358-8)

[Holt et al., Local translation in neuronal dendrites (2019) (2019)](https://doi.org/10.1016/j.neuron.2019.03.015)

[Wang et al., Translational deficits in Alzheimer's disease (2020) (2020)](https://doi.org/10.1016/j.neurobiolaging.2020.01.012)

[Hernandez et al., Amyloid-beta effects on ribosome function (2019) (2019)](https://doi.org/10.1016/j.jbc.100445)

[B福德 et al., Tau and translational control (2021) (2021)](https://doi.org/10.1016/j.neuropharm.2020.108236)

[Rugerio et al., Synaptic translation in memory formation (2022) (2022)](https://doi.org/10.1016/j.tics.2022.01.008)

[Linguin et al., Alpha-synuclein and ribosome dysfunction (2018) (2018)](https://doi.org/10.1002/mds.111)

[Giguère et al., Mitochondrial stress and translation (2019) (2019)](https://doi.org/10.1016/j.neurobiolaging.2019.05.014)

[Wakabayashi et al., Lewy body pathology and ribosomal proteins (2020) (2020)](https://doi.org/10.1111/nan.12654)

[Lo Cascio et al., Ribosomal dysfunction in ALS (2021) (2021)](https://doi.org/10.1007/s00401-021-02281-8)

[Mateju et al., Stress granules in neurodegeneration (2020) (2020)](https://doi.org/10.1083/jcb.202007123)

[Koch et al., Translational defects in Huntington's disease (2021) (2021)](https://doi.org/10.1093/brain/awab095)

[Cervera et al., Mutant huntingtin and ribosome function (2019) (2019)](https://doi.org/10.1093/hmg/ddz123)

[Brandman et al., Ribosome-associated quality control (2022) (2022)](https://doi.org/10.1146/annurev-biochem-040320-102821)

[Farrell et al., Oxidative stress and ribosome function (2018) (2018)](https://doi.org/10.1016/j.freeradbiomed.2018.02.032)

[Jansen et al., GWAS meta-analysis of Alzheimer's disease (2019) (2019)](https://doi.org/10.1038/s41586-019-1670-5)

[Nalls et al., Parkinson's disease GWAS (2019) (2019)](https://doi.org/10.1016/S1474-4422(19)

[Nicolas et al., ALS genetics and ribosomal proteins (2018) (2018)](https://doi.org/10.1101/362657)

[Neumann et al., TDP-43 proteinopathy in ALS and FTD (2020) (2020)](https://doi.org/10.1007/s00401-020-02187-3)

[Baker et al., Progranulin mutations in FTD (2021) (2021)](https://doi.org/10.1093/brain/awab095)

[Wolozin et al., Stress granules and neurodegeneration (2019) (2019)](https://doi.org/10.1016/j.neuron.2019.05.022)

[Dickson et al., Neuropathology of PSP (2020) (2020)](https://doi.org/10.1007/s00401-020-02174-w)

[Sztuk et al., DNA methylation in Alzheimer's disease (2019) (2019)](https://doi.org/10.1016/j.neurobiolaging.2019.03.011)

📖 View canonical wiki page →

Related Entities

RPL10A

▸Metadataorigin_type: v1_polymorphic_backfill

slug	genes-rpl10a
kg_node_id	RPL10A
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-e5302b00fd2e
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-rpl10a'}
_schema_version	1

📊 Evidence Profile Foundational

Evidence Balance

+0%

Certainty

55%

Debates

0

Incoming

11

Outgoing

23

0 supporting 0 contradicting 0 neutral

View full evidence profile →

Public annotations (0)Annotate on Hypothes.is →

No public annotations yet.

📗 Cite This Artifact

RPL10A — Ribosomal Protein L10A

RPL10A — Ribosomal Protein L10A

Overview

Gene Structure and Evolution

RPL10A — Ribosomal Protein L10A

Overview

Gene Structure and Evolution

Protein Structure and Biochemistry

Post-translational Modifications

Normal Cellular Function

Translation Regulation

Extra-ribosomal Functions

Expression Pattern

Role in Neurodegenerative Diseases

Alzheimer's Disease

Parkinson's Disease

Amyotrophic Lateral Sclerosis (ALS)

Huntington's Disease

Frontotemporal Dementia

Progressive Supranuclear Palsy

Amyotrophic Lateral Sclerosis (ALS)

Corticobasal Degeneration

Protein-Protein Interactions

Ribosomal Proteins

Translation Factors

Quality Control Proteins

Signaling Proteins

Disease-Related Proteins

Epigenetic Regulation

DNA Methylation

Histone Modifications

Non-coding RNAs

Clinical and Research Applications

Diagnostic Biomarkers

Prognostic Value

Therapeutic Monitoring

Molecular Mechanisms of Neurodegeneration

Ribosome Assembly Defects

Translational Fidelity

Ribosome-Associated Quality Control

Stress Response Integration

Genetic Associations and Variants

Alzheimer's Disease

Parkinson's Disease

ALS

Animal Models and Research

Mouse Models

Zebrafish Models

In vitro Models

Therapeutic Implications

Small Molecule Targeting

Gene Therapy Approaches

Small Molecules and Compounds

Biomarkers

Expression Biomarkers

Functional Biomarkers

Cross-linking and Related Pathways

Future Research Directions

Mermaid Diagram: Ribosomal Dysfunction in Neurodegeneration

See Also

External Links

References

💬 Discussion