{{.infobox .infobox-gene}}
| Symbol | RPS27L |
| Full Name | Ribosomal Protein S27 Like |
| Chromosome | 15q21.3 |
| NCBI Gene ID | 51065 |
| OMIM | 618199 |
| Ensembl ID | ENSG00000149691 |
| UniProt ID | Q9GZL0 |
| Associated Diseases | Cancer, Neurodegeneration |
Ribosomal Protein S27 Like (RPS27L) is a member of the ribosomal protein S27 family that plays essential roles in protein synthesis as a component of the 40S ribosomal subunit. Beyond its canonical function in translation, RPS27L has gained attention for its extraribosomal functions, particularly in p53-mediated apoptosis, cell cycle regulation, and stress response pathways[@warner2009][@zhou2015]. Dysregulation of RPS27L has been implicated in various diseases including cancer and neurodegenerative disorders.
RPS27L is highly conserved across eukaryotes and is expressed in most tissues with particularly high levels in the brain, where it participates in neuronal protein synthesis essential for synaptic plasticity and neuronal survival. The protein is encoded by the RPS27L gene located on chromosome 15q21.3.
RPS27L is a human gene. This page covers the gene's normal function, disease associations, expression patterns, and key research findings relevant to neurodegeneration.
The RPS27L gene spans approximately 4.5 kb and contains 5 exons. It encodes a 103-amino acid protein with a molecular weight of approximately 11 kDa.
RPS27L is a component of the 40S ribosomal subunit with:
| Feature | Function |
|---|---|
| RRM domain | RNA binding |
| Zinc finger motif | Metal binding and stability |
| Ribosomal binding site | Integration into 40S subunit |
The protein localizes to both the cytoplasm (ribosomal form) and nucleus (extraribosomal form), allowing it to participate in both translation and nuclear functions.
RPS27L shares high homology with RPS27 (RPS27), but has distinct functions:
As a component of the 40S ribosomal subunit, RPS27L participates in[@warren2012]:
RPS27L has several non-ribosomal functions[@uemura2010][@sun2018]:
p53 pathway: RPS27L directly interacts with p53 and promotes:
Cell cycle regulation: RPS27L affects:
Stress response: RPS27L responds to:
RPS27L exhibits broad but tissue-specific expression:
| Tissue | Expression Level | Notes |
|---|---|---|
| Brain | High | Neuronal expression |
| Liver | High | Metabolic function |
| Kidney | Moderate | Homeostasis |
| Heart | Moderate | Cardiac function |
| Testis | High | Spermatogenesis |
In neurons, RPS27L is localized in both the soma and dendritic compartments, where it supports local protein synthesis at synapses.
RPS27L is frequently dysregulated in cancer[@sun2018]:
RPS27L overexpression has been documented in:
RPS27L has emerging relevance to neurodegenerative diseases[@chen2020]:
Alzheimer's disease:
Parkinson's disease:
ALS:
Several RPS27L variants have been identified:
Somatic mutations in RPS27L have been found in:
[@warner2009]: Warner JR, McIntosh KB. How common are extraribosomal functions of ribosomal proteins?. Mol Cell. 2009;34(1):3-11.
[@warren2012]: Warren AJ. Eukaryotic translation initiation factors and ribosome biogenesis in cancer. Front Oncol. 2012;2:105.
[@khodorov2002]: Khodorov B, et al. Protein synthesis in neurons and the mechanism of learning. Neuroscience. 2002;115(4):973-977.
[@ding2005]: Ding Q, et al. Regulation of neuronal survival by ribosomal proteins. J Exp Med. 2005;202(1):119-127.
[@besse2011]: Besse F, et al. The Drosophila ribosomal protein L27 leads to synaptic growth. PLoS One. 2011;6(7):e22501.
[@zhou2015]: Zhou X, et al. Ribosomal proteins: functions beyond the ribosome. J Mol Cell Biol. 2015;7(2):92-104.
[@uemura2010]: Uemura M, et al. Direct interaction between RPS27L and p53. Cell Cycle. 2010;9(19):3935-3943.
[@sun2018]: Sun X, et al. RPS27L promotes cell proliferation and inhibits apoptosis in cancer. Oncogene. 2018;37(27):3622-3634.
[@zhang2019]: Zhang W, et al. RPS27L regulates ribosomal protein homeostasis and translation. J Cell Sci. 2019;132(10):jcs228346.
[@chen2020]: Chen J, et al. Ribosomal proteins and neurodegeneration: emerging mechanisms. Trends Neurosci. 2020;43(5):331-342.
[@liu2021]: Liu H, et al. RPS27L in stress response and cellular adaptation. Cell Stress Chaperones. 2021;26(4):623-633.