scholarly journals Colocalization of MID1IP1 and c-Myc is Critically Involved in Liver Cancer Growth via Regulation of Ribosomal Protein L5 and L11 and CNOT2

Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 985 ◽  
Author(s):  
Ji Hoon Jung ◽  
Hyo-Jung Lee ◽  
Ju-Ha Kim ◽  
Deok Yong Sim ◽  
Eunji Im ◽  
...  
Keyword(s):  
Liver Cancer ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Tissue Array ◽  
Interacting Protein ◽  
Normal Hepatocyte ◽  
Huh7 Cells ◽  
Element Binding Protein ◽  
Ribosomal Protein L5 ◽  
Underlying Mechanisms

Though midline1 interacting protein 1 (MID1IP1) was known as one of the glucose-responsive genes regulated by carbohydrate response element binding protein (ChREBP), the underlying mechanisms for its oncogenic role were never explored. Thus, in the present study, the underlying molecular mechanism of MID1P1 was elucidated mainly in HepG2 and Huh7 hepatocellular carcinoma cells (HCCs). MID1IP1 was highly expressed in HepG2, Huh7, SK-Hep1, PLC/PRF5, and immortalized hepatocyte LX-2 cells more than in normal hepatocyte AML-12 cells. MID1IP1 depletion reduced the viability and the number of colonies and also increased sub G1 population and the number of TUNEL-positive cells in HepG2 and Huh7 cells. Consistently, MID1IP1 depletion attenuated pro-poly (ADP-ribose) polymerase (pro-PARP), c-Myc and activated p21, while MID1IP1 overexpression activated c-Myc and reduced p21. Furthermore, MID1IP1 depletion synergistically attenuated c-Myc stability in HepG2 and Huh7 cells. Of note, MID1IP1 depletion upregulated the expression of ribosomal protein L5 or L11, while loss of L5 or L11 rescued c-Myc in MID1IP1 depleted HepG2 and Huh7 cells. Interestingly, tissue array showed that the overexpression of MID1IP1 was colocalized with c-Myc in human HCC tissues, which was verified in HepG2 and Huh7 cells by Immunofluorescence. Notably, depletion of CCR4-NOT2 (CNOT2) with adipogenic activity enhanced the antitumor effect of MID1IP1 depletion to reduce c-Myc, procaspase 3 and pro-PARP in HepG2, Huh7 and HCT116 cells. Overall, these findings provide novel insight that MID1IP1 promotes the growth of liver cancer via colocalization with c-Myc mediated by ribosomal proteins L5 and L11 and CNOT2 as a potent oncogenic molecule.

Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5

1989 ◽  
Vol 9 (12) ◽  
pp. 5281-5288
Author(s):  
W M Wormington
Keyword(s):  
Ribosomal Protein ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
5S Rrna ◽  
Yeast Cells ◽  
Developmental Expression ◽  
Rrna Synthesis ◽  
Ribosome Assembly ◽  
Subunit Assembly ◽  
Ribosomal Protein L5

Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.

scholarly journals p53-Dependent Apoptotic Effect of Puromycin via Binding of Ribosomal Protein L5 and L11 to MDM2 and its Combination Effect with RITA or Doxorubicin

Cancers ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 582 ◽  
Author(s):  
Jung ◽  
Lee ◽  
Kim ◽  
Sim ◽  
Ahn ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Cancer Cells ◽  
Ribosomal Proteins ◽  
Antitumor Effect ◽  
Wild Type ◽  
Diphenyltetrazolium Bromide ◽  
Apoptotic Effect ◽  
Ribosomal Protein L5 ◽  
Proliferation Assays ◽  
Hct116 Cells

Among ribosomal proteins essential for protein synthesis, the functions of ribosomal protein L5 (RPL5) and RPL11 still remain unclear to date. Here, the roles of RPL5 and RPL11 were investigated in association with p53/p21 signaling in the antitumor effect of puromycin mainly in HCT116 and H1299 cancer cells. Cell proliferation assays using 3-[4,5-dimethylthiazole-2-yl]-2,5-diphenyltetrazolium bromide (MTT) assays and colony formation assays, cell cycle analysis, Reverse transcription polymerase chain reaction (RT-PCR) and Western blotting were performed in cancer cells. Puromycin exerted cytotoxic and anti-proliferative effects in p53 wild-type HCT116 more than in p53 null H1299 cells. Consistently, puromycin increased sub-G1, cleaved Poly (ADP-ribose) polymerase (PARP), activated p53, p21, and Mouse double minute 2 homolog (MDM2), and attenuated expression of c-Myc in HCT116 cells. Notably, puromycin upregulated the expression of RPL5 and RPL11 to directly bind to MDM2 in HCT116 cells. Conversely, deletion of RPL5 and RPL11 blocked the activation of p53, p21, and MDM2 in HCT116 cells. Also, puromycin enhanced the antitumor effect with reactivating p53 and inducing tumor apoptosis (RITA) or doxorubicin in HCT116 cells. These findings suggest that puromycin induces p53-dependent apoptosis via upregulation of RPL5 or RPL11 for binding with MDM2, and so can be used more effectively in p53 wild-type cancers by combination with RITA or doxorubicin.

scholarly journals Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5.

1989 ◽  
Vol 9 (12) ◽  
pp. 5281-5288 ◽  
Author(s):  
W M Wormington
Keyword(s):  
Ribosomal Protein ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
5S Rrna ◽  
Yeast Cells ◽  
Developmental Expression ◽  
Rrna Synthesis ◽  
Ribosome Assembly ◽  
Subunit Assembly ◽  
Ribosomal Protein L5

Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.

scholarly journals Ribosome Biogenesis in African Trypanosomes Requires Conserved and Trypanosome-Specific Factors

2014 ◽  
Vol 13 (6) ◽  
pp. 727-737 ◽  
Author(s):  
Khan Umaer ◽  
Martin Ciganda ◽  
Noreen Williams
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Large Subunit ◽  
Ribosomal Subunit ◽  
Small Subunit ◽  
5S Rrna ◽  
Content Type ◽  
African Trypanosomes ◽  
Ribosomal Protein L5

ABSTRACTLarge ribosomal subunit protein L5 is responsible for the stability and trafficking of 5S rRNA to the site of eukaryotic ribosomal assembly. InTrypanosoma brucei, in addition to L5, trypanosome-specific proteins P34 and P37 also participate in this process. These two essential proteins form a novel preribosomal particle through interactions with both the ribosomal protein L5 and 5S rRNA. We have generated a procyclic L5 RNA interference cell line and found that L5 itself is a protein essential for trypanosome growth, despite the presence of other 5S rRNA binding proteins. Loss of L5 decreases the levels of all large-subunit rRNAs, 25/28S, 5.8S, and 5S rRNAs, but does not alter small-subunit 18S rRNA. Depletion of L5 specifically reduced the levels of the other large ribosomal proteins, L3 and L11, whereas the steady-state levels of the mRNA for these proteins were increased. L5-knockdown cells showed an increase in the 40S ribosomal subunit and a loss of the 60S ribosomal subunits, 80S monosomes, and polysomes. In addition, L5 was involved in the processing and maturation of precursor rRNAs. Analysis of polysomal fractions revealed that unprocessed rRNA intermediates accumulate in the ribosome when L5 is depleted. Although we previously found that the loss of P34 and P37 does not result in a change in the levels of L5, the loss of L5 resulted in an increase of P34 and P37 proteins, suggesting the presence of a compensatory feedback loop. This study demonstrates that ribosomal protein L5 has conserved functions, in addition to nonconserved trypanosome-specific features, which could be targeted for drug intervention.

Functional amyloid: widespread in Nature, diverse in purpose

2014 ◽  
Vol 56 ◽  
pp. 207-219 ◽  
Author(s):  
Chi L.L. Pham ◽  
Ann H. Kwan ◽  
Margaret Sunde
Keyword(s):  
Spider Silk ◽  
Epigenetic Inheritance ◽  
Fibrillar Structure ◽  
Cytoplasmic Polyadenylation ◽  
Functional Amyloid ◽  
Interacting Protein ◽  
Diverse Range ◽  
Element Binding Protein ◽  
Functional Amyloids ◽  
Micro Organisms

Amyloids are insoluble fibrillar protein deposits with an underlying cross-β structure initially discovered in the context of human diseases. However, it is now clear that the same fibrillar structure is used by many organisms, from bacteria to humans, in order to achieve a diverse range of biological functions. These functions include structure and protection (e.g. curli and chorion proteins, and insect and spider silk proteins), aiding interface transitions and cell–cell recognition (e.g. chaplins, rodlins and hydrophobins), protein control and storage (e.g. Microcin E492, modulins and PMEL), and epigenetic inheritance and memory [e.g. Sup35, Ure2p, HET-s and CPEB (cytoplasmic polyadenylation element-binding protein)]. As more examples of functional amyloid come to light, the list of roles associated with functional amyloids has continued to expand. More recently, amyloids have also been implicated in signal transduction [e.g. RIP1/RIP3 (receptor-interacting protein)] and perhaps in host defence [e.g. aDrs (anionic dermaseptin) peptide]. The present chapter discusses in detail functional amyloids that are used in Nature by micro-organisms, non-mammalian animals and mammals, including the biological roles that they play, their molecular composition and how they assemble, as well as the coping strategies that organisms have evolved to avoid the potential toxicity of functional amyloid.

scholarly journals Molecular cloning and nucleotide sequence of cDNA specific for rat ribosomal protein L5

1987 ◽  
Vol 168 (1) ◽  
pp. 83-87 ◽  
Author(s):  
Satoru TAMURA ◽  
Yuh KUWANO ◽  
Tatsuo NAKAYAMA ◽  
Shoji TANAKA ◽  
Tatsuo TANAKA ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Ribosomal Protein ◽  
Molecular Cloning ◽  
Ribosomal Protein L5

The N-terminal Sequence of Ribosomal Protein L10 from the ArchaebacteriumHalobacterium marismortuiand its Relationship to Eubacterial Protein L6 and Other Ribosomal Proteins

1987 ◽  
Vol 368 (2) ◽  
pp. 921-926 ◽  
Author(s):  
Jan DIJK ◽  
Rudolf VAN DEN BROEK ◽  
Georgios NASIULAS ◽  
Alfred BECK ◽  
Richard REINHARDT ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Terminal Sequence

scholarly journals Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid

1972 ◽  
Vol 130 (1) ◽  
pp. 103-110 ◽  
Author(s):  
L. P. Visentin ◽  
C. Chow ◽  
A. T. Matheson ◽  
M. Yaguchi ◽  
F. Rollin
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Soluble Fraction ◽  
Ribosomal Subunit ◽  
23S Rrna ◽  
Core Particle ◽  
Fractionation Procedure ◽  
Additional Protein ◽  
70S Ribosome ◽  
Low Ionic Strength

1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K+ and 0.1m-Mg2+, were extracted with low-ionic-strength buffer 75–80% of the 30S proteins and 60–65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li+–EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%).

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