Negative charge in the RACK1 loop broadens the translational capacity of the human ribosome

Rollins, Madeline G.; Shasmal, Manidip; Meade, Nathan; Astar, Helen; Shen, Peter; Walsh, Derek

doi:10.1016/j.celrep.2021.109663

Cited by 15 publications

(4 citation statements)

References 122 publications

(200 reference statements)

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“…With respect to RP or rRNA modifications, vaccinia virus stimulates the phosphorylation of uS5/RPS2, which is near the mRNA entry channel, and the phosphorylation of RACK1 near the mRNA exit channel, resulting in a ribosomal preference for A-rich 5′ UTRs characteristic of poxviruses [ 166 , 167 ]. Additionally, ubiquitination of uS10/RPS20 is required for poxvirus translation [ 168 ].…”

Section: Disease-associated Ribosomal Heterogeneity and Specializationmentioning

confidence: 99%

Specialized Ribosomes in Health and Disease

Miller

MacDonald

Kellogg

et al. 2023

IJMS

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Ribosomal heterogeneity exists within cells and between different cell types, at specific developmental stages, and occurs in response to environmental stimuli. Mounting evidence supports the existence of specialized ribosomes, or specific changes to the ribosome that regulate the translation of a specific group of transcripts. These alterations have been shown to affect the affinity of ribosomes for certain mRNAs or change the cotranslational folding of nascent polypeptides at the exit tunnel. The identification of specialized ribosomes requires evidence of the incorporation of different ribosomal proteins or of modifications to rRNA and/or protein that lead(s) to physiologically relevant changes in translation. In this review, we summarize ribosomal heterogeneity and specialization in mammals and discuss their relevance to several human diseases.

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Section: Disease-associated Ribosomal Heterogeneity and Specializationmentioning

confidence: 99%

Specialized Ribosomes in Health and Disease

Miller

MacDonald

Kellogg

et al. 2023

IJMS

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show abstract

“…4 ) phosphorylation, VacV remodels ribosome transcript selectivity. The resulting negative charge on RACK1 Ser/Thr residues within an extended loop increases the swivel motion of the 40S head domain and broadens the translational capacity of the human ribosome, enabling preferential translation of viral mRNAs containing A-rich 5′ UTRs ( Jha et al 2017 ; Rollins et al 2021 ). Finally, ubiquitin fold modifier (UFM1) conjugation to uL24 (RPL26) ( Fig.…”

Section: Appropriating Host Ribosomes In Virus-infected Cellsmentioning

confidence: 99%

Minding the message: tactics controlling RNA decay, modification, and translation in virus-infected cells

2022

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With their categorical requirement for host ribosomes to translate mRNA, viruses provide a wealth of genetically tractable models to investigate how gene expression is remodeled post-transcriptionally by infection-triggered biological stress. By co-opting and subverting cellular pathways that control mRNA decay, modification, and translation, the global landscape of post-transcriptional processes is swiftly reshaped by virus-encoded factors. Concurrent host cell-intrinsic countermeasures likewise conscript post-transcriptional strategies to mobilize critical innate immune defenses. Here we review strategies and mechanisms that control mRNA decay, modification, and translation in animal virus-infected cells. Besides settling infection outcomes, post-transcriptional gene regulation in virus-infected cells epitomizes fundamental physiological stress responses in health and disease.

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“…Different viral infections lead to various phosphorylation modifications of the ribosomal protein; this facilitates the expression of viral proteins ( DiGiuseppe et al, 2020 ). Regarding phosphorylation of RACK1, researchers suggest that mutation of the phosphorylation site in the RACK1 protein to a negatively charged amino acid not only results in a conformational change in the 80S ribosomal subunit and a change in the conformation of the 40S ribosomal head, but it also promotes viral protein translation ( Rollins et al, 2021 ). In summary, viral infection and modification of ribosomal components lead to heterogeneity of ribosomal function and promote the expression of viral proteins.…”

Section: Viruses Hijack Ribosomes To Complete Viral Protein Translationmentioning

confidence: 99%

Ribosomal control in RNA virus-infected cells

et al. 2022

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Viruses are strictly intracellular parasites requiring host cellular functions to complete their reproduction cycle involving virus infection of host cell, viral genome replication, viral protein translation, and virion release. Ribosomes are protein synthesis factories in cells, and viruses need to manipulate ribosomes to complete their protein synthesis. Viruses use translation initiation factors through their own RNA structures or cap structures, thereby inducing ribosomes to synthesize viral proteins. Viruses also affect ribosome production and the assembly of mature ribosomes, and regulate the recognition of mRNA by ribosomes, thereby promoting viral protein synthesis and inhibiting the synthesis of host antiviral immune proteins. Here, we review the remarkable mechanisms used by RNA viruses to regulate ribosomes, in particular, the mechanisms by which RNA viruses induce the formation of specific heterogeneous ribosomes required for viral protein translation. This review provides valuable insights into the control of viral infection and diseases from the perspective of viral protein synthesis.

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Negative charge in the RACK1 loop broadens the translational capacity of the human ribosome

Cited by 15 publications

References 122 publications

Specialized Ribosomes in Health and Disease

Specialized Ribosomes in Health and Disease

Minding the message: tactics controlling RNA decay, modification, and translation in virus-infected cells

Ribosomal control in RNA virus-infected cells

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