Late-assembly of human ribosomal protein S20 in the cytoplasm is essential for the functioning of the small subunit ribosome

Tai, Lin-Ru; Chou, Chang-Wei; Wu, Jing-Ying; Kirby, Ralph; Lin, Alan

doi:10.1016/j.yexcr.2013.09.013

Cited by 3 publications

(3 citation statements)

References 31 publications

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“…RPS20 isoform 1 contains 142 amino acids while isoform 2 encodes 119 amino acids. Previous report suggests that RPS20 play an important role in ribosomal RNA processing 33 and predominantly localized in cytoplasm 34 which is distinct from other ribosomal proteins that are commonly found in nucleolus 35 – 40 . Recent studies provided clear evidence that several ribosomal proteins play a critical role in the regulation of ‘non-ribosomal function’ like modulating p53-MDM2 pathways to promote cell proliferation during tumorigenesis 41 – 52 .…”

Section: Discussionmentioning

confidence: 96%

Interplay between human nucleolar GNL1 and RPS20 is critical to modulate cell proliferation

Krishnan

Boddapati

Mahalingam

2018

Sci Rep

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Human Guanine nucleotide binding protein like 1 (GNL1) belongs to HSR1_MMR1 subfamily of nucleolar GTPases. Here, we report for the first time that GNL1 promotes cell cycle and proliferation by inducing hyperphosphorylation of retinoblastoma protein. Using yeast two-hybrid screening, Ribosomal protein S20 (RPS20) was identified as a functional interacting partner of GNL1. Results from GST pull-down and co-immunoprecipitation assays confirmed that interaction between GNL1 and RPS20 was specific. Further, GNL1 induced cell proliferation was altered upon knockdown of RPS20 suggesting its critical role in GNL1 function. Interestingly, cell proliferation was significantly impaired upon expression of RPS20 interaction deficient GNL1 mutant suggest that GNL1 interaction with RPS20 is critical for cell growth. Finally, the inverse correlation of GNL1 and RPS20 expression in primary colon and gastric cancers with patient survival strengthen their critical importance during tumorigenesis. Collectively, our data provided evidence that cross-talk between GNL1 and RPS20 is critical to promote cell proliferation.

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Section: Discussionmentioning

confidence: 96%

Interplay between human nucleolar GNL1 and RPS20 is critical to modulate cell proliferation

Krishnan

Boddapati

Mahalingam

2018

Sci Rep

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“…4E, G), suggesting that the ubiquitination of RPS20 more likely plays a role in regulation than it does in protein degradation. Studies have indicated that RPS20 ubiquitination is critical to the regulation of the assembly of the 40S ribosomal subunit and the translation of speci c mRNAs 58,59 and it is also involved in various cellular functions, including ribosome biogenesis, mRNA translation, and protein quality control 51,55,56 . In this study, the immunoprecipitation of RPS20 from mitochondrial fraction showed that most of the RPS20 proteins were monoubiquitinated in KB cells, suggesting that monoubiquitinated RPS20 is essential for the proper translation on mitochondria associated ribosomes.…”

Section: Discussionmentioning

confidence: 99%

Targeting ZAKα Interactions and Ribosomes with Novel peptides: The role of ZAKα in Mitochondrial Function and Cancer Cell Proliferation

Yang,

Hsu,

Yeh

2024

Preprint

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Phage display was used to identify high-affinity and high-specificity peptides that might inhibit ZAKα, a kinase implicated in cellular proliferation, differentiation, and stress response and implicated in both malignant tumor growth and metastasis as well as the pathogenesis of cardiac hypertrophy and fibrotic heart disease. Two peptides were found to specifically bind to ZAKα, PhD30 and PhD35. Their introduction into cancer cells led to the dissociation of ZAKα from RPS20 and the ubiquitination of RPS20 protein resulting in a reduction of essential mitochondria proteins and mitochondria activity impeding the translation of mitochondrial-associated eukaryotic ribosomes, a process we believe to be crucial for tumor growth. This mechanism of action suggests that the primary effect of PhD30 and PhD35 is to lower mitochondrial activity by causing a shortage of essential proteins in mitochondria without changing the number of apoptotic and necrotic cancer cells. Thus, these findings may prove pivotal to the development of a novel approach utilizing these peptides to inhibit cancer cell growth by targeting mitochondrial function, rather than the conventional method of inducing apoptosis.

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“…RPS20 is mainly involved in the regulation of ribosomal RNA processing (10). It is primarily localized in the cytoplasm (11), unlike other RPs, which are usually found in the nucleoli (12)(13)(14)(15)(16)(17). Recent evidence suggested that RPS20 is involved in non-ribosomal regulation.…”

Section: Introductionmentioning

confidence: 99%

Biochemical and clinical effects of RPS20 expression in renal clear cell carcinoma

et al. 2022

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Renal cell carcinoma (RCC) remains one of the most lethal urinary tumors in East Asia despite great advancements in treatment strategies in recent years. Ribosomal protein S20 (RPS20) is considered a new oncogene; however, little information is available on its expression, regulation and biological function in patients with RCC. In the present study, 43 pairs of human RCC and neighboring normal renal tissues were examined for protein expression and immunohistochemistry examination of RPS20. Lentiviral transduction was also employed to create RPS20 knockdown cell lines for downstream cellular experiments. MTT, flow cytometry, wound healing, colony formation and invasion assays were used to examine how RPS20 affected kidney renal clear cell carcinoma (KIRC) cell behavior. Western blotting was used to detect cycle-related proteins (CDK4 and cyclin D1), Wnt-related proteins (N-cadherin and E-cadherin) and signaling proteins [phosphorylated (p)-AKT and p-ERK]. The functions of RPS20 in vivo were examined in 786-O cells with RPS20 knockdown. RPS20 was significantly overexpressed in tumor tissues compared with its expression in the corresponding normal tissues. RPS20 expression was linked to tumor stage, differentiation grade, tumor size and lymph node metastasis, and it had an independent prognostic value in KIRC. Since RCC cell proliferation, migration and invasion were suppressed when RPS20 was knocked down, the formation of renal tumors in vivo was markedly slowed down. In RPS20 knockdown cell lines, CDK4, cyclin D1 and E-cadherin were downregulated, while N-cadherin expression was increased. RPS20 was also observed to be involved in controlling the activation of the ERK and mTOR signaling pathways. In summary, the present study showed that RPS20 increased cell proliferation in RCC by activating the AKT-mTOR and ERK-MAPK signaling pathways, which suggests that RPS20 may be a therapeutic and prognostic target for RCC.

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Late-assembly of human ribosomal protein S20 in the cytoplasm is essential for the functioning of the small subunit ribosome

Cited by 3 publications

References 31 publications

Interplay between human nucleolar GNL1 and RPS20 is critical to modulate cell proliferation

Interplay between human nucleolar GNL1 and RPS20 is critical to modulate cell proliferation

Targeting ZAKα Interactions and Ribosomes with Novel peptides: The role of ZAKα in Mitochondrial Function and Cancer Cell Proliferation

Biochemical and clinical effects of RPS20 expression in renal clear cell carcinoma

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