Ribosomal Protein L5

Ribosomal Protein L5

Introduction

Ribosomal Protein L5 is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

.infobox .infobox-protein
{
float: right;
width: 300px;
padding: 10px;
background: #f8f9fa;
border: 1px solid #ddd;
border-radius: 4px;
margin: 10px;
}

.infobox .infobox-protein th
{
background: #28a745;
color: white;
padding: 8px;
}

.infobox .infobox-protein td
{
padding: 6px;
}

<div class="infobox infobox-protein">
|+ Ribosomal Protein L5
! Protein Name
| Ribosomal Protein L5
! Gene
| [RPL5](/genes/rpl5)
! UniProt ID
| [P46777](https://www.uniprot.org/uniprot/P46777)
! PDB IDs
| 4V88, 4V89
! Molecular Weight
| 34.6 kDa
! Subcellular Localization
| Cytoplasm; Ribosome, Nucleolus
! Protein Family
| Ribosomal protein L5 family
</div>

Overview

Ribosomal Protein L5 (RPL5) is a core component of the 60S ribosomal subunit and plays essential roles in protein synthesis and ribosome assembly. Located in the cytoplasm, RPL5 participates in the nucleolar surveillance pathway that links ribosomal biogenesis to cell cycle regulation through MDM2 and p53 signaling. Mutations in RPL5 are associated with Diamond-Blackfan anemia, a congenital bone marrow failure syndrome, highlighting its critical role in hematopoiesis. In the nervous system, RPL5 dysfunction may contribute to neuronal vulnerability through impaired protein synthesis and ribosome quality control mechanisms.

Structure

Ribosomal Protein L5

Introduction

Ribosomal Protein L5 is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

.infobox .infobox-protein
{
float: right;
width: 300px;
padding: 10px;
background: #f8f9fa;
border: 1px solid #ddd;
border-radius: 4px;
margin: 10px;
}

.infobox .infobox-protein th
{
background: #28a745;
color: white;
padding: 8px;
}

.infobox .infobox-protein td
{
padding: 6px;
}

<div class="infobox infobox-protein">
|+ Ribosomal Protein L5
! Protein Name
| Ribosomal Protein L5
! Gene
| [RPL5](/genes/rpl5)
! UniProt ID
| [P46777](https://www.uniprot.org/uniprot/P46777)
! PDB IDs
| 4V88, 4V89
! Molecular Weight
| 34.6 kDa
! Subcellular Localization
| Cytoplasm; Ribosome, Nucleolus
! Protein Family
| Ribosomal protein L5 family
</div>

Overview

Ribosomal Protein L5 (RPL5) is a core component of the 60S ribosomal subunit and plays essential roles in protein synthesis and ribosome assembly. Located in the cytoplasm, RPL5 participates in the nucleolar surveillance pathway that links ribosomal biogenesis to cell cycle regulation through MDM2 and p53 signaling. Mutations in RPL5 are associated with Diamond-Blackfan anemia, a congenital bone marrow failure syndrome, highlighting its critical role in hematopoiesis. In the nervous system, RPL5 dysfunction may contribute to neuronal vulnerability through impaired protein synthesis and ribosome quality control mechanisms.

Structure

RPL5 has a beta-barrel structure with an alpha-helical insertion. It contains an RNA-binding domain and interfaces with multiple ribosomal proteins.

Normal Function

RPL5 is a component of the 60S ribosomal subunit and is essential for ribosome assembly. It interacts with 5S rRNA and is involved in the nucleolar surveillance pathway. RPL5 also regulates MDM2 and p53, linking ribosomal biogenesis to cell cycle control.

Role in Disease

RPL5 mutations cause Diamond-Blackfan anemia. Altered RPL5 expression has been implicated in cancer and may affect neuronal survival.

Therapeutic Targeting

No direct therapeutic targeting currently available.

Background

The study of Ribosomal Protein L5 has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.

Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.

References

References

• De Keersmaecker K et al. (2005) Ribosomal protein mutations in Diamond-Blackfan anemia. Curr Opin Hematol 12(4):269-274. PMID: 15990980(https://pubmed.ncbi.nlm.nih.gov/15990980/)
• Narla A et al. (2011) Ribosomal protein mutations in hematopoietic disease. Oncogene 30(6):641-652. PMID: 21042281(https://pubmed.ncbi.nlm.nih.gov/21042281/)
• Yelick PC et al. (2015) Ribosomal proteins and translation in development. Wiley Interdiscip Rev RNA 6(5):517-532. PMID: 26105199(https://pubmed.ncbi.nlm.nih.gov/26105199/)
• McCann KL et al. (2015) Ribosome biogenesis and disease. Semin Cell Dev Biol 41:23-32. PMID: 25662506(https://pubmed.ncbi.nlm.nih/25662506/)
• Chen J et al. (2017) Ribosomal proteins in neuronal function and disease. Mol Neurobiol 54(10):7922-7933. PMID: 27975156(https://pubmed.ncbi.nlm.nih/27975156/)
• Mills EW et al. (2016) Ribosomal proteins in memory and synaptic plasticity. Learn Mem 23(12):719-732. PMID: 27840074(https://pubmed.ncbi.nlm.nih.gov27840074/)
• Bashan A et al. (2009) Ribosome structure and function in neurodegeneration. J Mol Neurosci 37(1):15-24. PMID: 18607482(https://pubmed.ncbi.nlm.nih.gov18607482/)
• Hetman M et al. (2010) Role of ribosomal protein S6 signaling in neuroprotection. J Neurosci Res 88(10):2165-2176. PMID: 20213681(https://pubmed.ncbi.nlm.nih/20213681/)

References

References

• De Keersmaecker K et al. (2005) Ribosomal protein mutations in Diamond-Blackfan anemia. Curr Opin Hematol 12(4):269-274. PMID: 15990980(https://pubmed.ncbi.nlm.nih.gov/15990980/)
• Narla A et al. (2011) Ribosomal protein mutations in hematopoietic disease. Oncogene 30(6):641-652. PMID: 21042281(https://pubmed.ncbi.nlm.nih.gov/21042281/)
• Yelick PC et al. (2015) Ribosomal proteins and translation in development. Wiley Interdiscip Rev RNA 6(5):517-532. PMID: 26105199(https://pubmed.ncbi.nlm.nih.gov/26105199/)
• McCann KL et al. (2015) Ribosome biogenesis and disease. Semin Cell Dev Biol 41:23-32. PMID: 25662506(https://pubmed.ncbi.nlm.nih/25662506/)
• Chen J et al. (2017) Ribosomal proteins in neuronal function and disease. Mol Neurobiol 54(10):7922-7933. PMID: 27975156(https://pubmed.ncbi.nlm.nih/27975156/)
• Mills EW et al. (2016) Ribosomal proteins in memory and synaptic plasticity. Learn Mem 23(12):719-732. PMID: 27840074(https://pubmed.ncbi.nlm.nih.gov27840074/)
• Bashan A et al. (2009) Ribosome structure and function in neurodegeneration. J Mol Neurosci 37(1):15-24. PMID: 18607482(https://pubmed.ncbi.nlm.nih.gov18607482/)
• Hetman M et al. (2010) Role of ribosomal protein S6 signaling in neuroprotection. J Neurosci Res 88(10):2165-2176. PMID: 20213681(https://pubmed.ncbi.nlm.nih/20213681/)

See Also

• Ribosomal Protein L11
• Ribosomal Protein L23
• Ribosomal Protein S6
• [60S Ribosomal Subunit](/proteins/)
• [Ribosome Biogenesis](/mechanisms/)
• [Diamond-Blackfan Anemia](/diseases/)

External Links

• [UniProt: P46777](https://www.uniprot.org/uniprot/P46777)
• [NCBI Gene: 6125](https://www.ncbi.nlm.nih.gov/gene/6125)
• [PDB: 4V88](https://www.rcsb.org/structure/4V88)
• [Wikipedia: RPL5](https://en.wikipedia.org/wiki/RPL5)