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RPL5 remains an interesting candidate in multiple myelom(MM )because it is deleted in 20-40% of MM cases
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Whole exome sequencing in the differential diagnosis of Diamond-Blackfan anemia: Clinical and molecular study of three patients with novel RPL5 and mosaic RPS19 mutations
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Low RPL5 expression is associated with cancer.
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Ribosomal proteins L11 and L5 activate TAp73 by overcoming MDM2 inhibition.
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RPL5 mutation is associated with Diamond Blackfan Anemia.
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Findings uncover a mechanism by which RPL5 and RPL11 can co-operatively suppress c-Myc expression, allowing a tightly controlled ribosome biogenesis in cells.
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Unlike other tumor suppressors, RPL5 and RPL11 play essential roles in normal cell proliferation.
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High frequency of RPL5 gene deletion is associated with Italian Diamond-Blackfan anemia.
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Oncogenic splicing factor SRSF1 stabilizes the tumor suppressor protein p53 via RPL5, inducing cell senescence.
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Mutations affect the ribosomal proteins RPL5 and RPL10 in 12 of 122 (9.8%) pediatric T-cell acute lymphoblastic leukemias.
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disrupted nucleoli may provide a platform for L5- and L11-dependent p53 activation, implying a role for the nucleolus in p53 activation by ribosomal biogenesis stress
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Data show 1 proband with an RPL5 deletion, 1 patient with an RPL35A deletion, 3 with RPS17 deletions, and 1 with an RPS19 deletion.
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Data show that all patients with RPS19 and RPL5 mutations had physical abnormalities.
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An analysis and fine mapping of GFI-EVI5-RPL5-FAM69A locus, genotyping eight Tag-single nucleotide polymorphisms in 732 multiple sclerosis patients and 974 controls from Spain, was performed.
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Knockdown of L29 or L30 enhanced the interaction of MDM2 with L11 and L5 and markedly inhibited MDM2-mediated p53 ubiquitination, suggesting that direct perturbation of 60 S ribosomal biogenesis activates p53 via L11- and L5-mediated MDM2 suppression.
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The study reports a high frequency of RPL5 (9.3%) and RPL11 (9.3%) mutations in a Diamond-Blackfan anemia cohort.
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the presence of multiple NLSs in ribosomal protein L5 appears to allow for efficient nuclear transport via utilisation of multiple, mechanistically different import pathways.
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the MDM2-L5-L11-L23 complex functions to inhibit MDM2-mediated p53 ubiquitination and thus activates p53
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interaction of NVL2 with L5 is ATP-dependent and likely contributes to the nucleolar translocation of NVL2
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Cancer-associated missense mutations targeting MDM2's central zinc finger disrupt the interaction of MDM2 with L5 and L11.
