Immune Responses – Transcriptional and Post-Transcriptional Networks Pass the Baton

Lichti, Johannes; Gallus, Christian; Glasmacher, Elke

doi:10.1016/j.tibs.2017.11.003

Cited by 6 publications

(7 citation statements)

References 13 publications

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“…Several previous results offered early clues that mechanisms may operate to couple NPET construction with other remodeling events during 60S subunit assembly 5 , 40 , 41 . For example, translating ribosomes that are stalled in response to small molecules, peptides, or antibiotics that bind to the NPET display a distorted PTC incapable of catalyzing peptide bond formation 4 . Furthermore, defects in bacterial ribosomes lacking a 5S RNP can be partially rescued by the binding of a macrolide antibiotic, which binds to the NPET 42 .…”

Section: Discussionmentioning

confidence: 99%

“…The NPET is the 90 angstrom-long conduit through which all nascent polypeptide chains travel from the PTC to the exterior of the 60S subunit 3 . It has become increasingly clear that the NPET functions as a sensor of both specific sequences in nascent polypeptides and small molecule effectors, including antibiotics, to modulate the activity of the PTC and regulate the synthesis of specific subsets of proteins 4 – 6 . The physicochemical properties of the NPET have also been shown to actively affect protein folding 7 .…”

Section: Introductionmentioning

confidence: 99%

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Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel

et al. 2020

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The nascent polypeptide exit tunnel (NPET) is a major functional center of 60S ribosomal subunits. However, little is known about how the NPET is constructed during ribosome assembly. We utilized molecular genetics, biochemistry, and cryo-electron microscopy (cryo-EM) to investigate the functions of two NPET-associated proteins, ribosomal protein uL4 and assembly factor Nog1, in NPET assembly. Structures of mutant pre-ribosomes lacking the tunnel domain of uL4 reveal a misassembled NPET, including an aberrantly flexible ribosomal RNA helix 74, resulting in at least three different blocks in 60S assembly. Structures of pre-ribosomes lacking the C-terminal extension of Nog1 demonstrate that this extension scaffolds the tunnel domain of uL4 in the NPET to help maintain stability in the core of pre-60S subunits. Our data reveal that uL4 and Nog1 work together in the maturation of ribosomal RNA helix 74, which is required to ensure proper construction of the NPET and 60S ribosomal subunits.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel

et al. 2020

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“…RNA-regulating factors have various key functions within immune cells that are just beginning to be understood (Lichti et al, 2018). Depending on species, between 2% and 10% of all coding genes are believed to bind RNA (Lasko, 2000; Gerstberger et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…The anti-inflammatory pathways that ensure immune homeostasis are just beginning to be understood. RNA-regulating factors and posttranscriptional networks are known to play a particularly important role in the interplay between pro- and anti-inflammatory pathways (Lichti et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Immune homeostasis and regulation of the interferon pathway require myeloid-derived Regnase-3

Gamm

Schaub

Jones

et al. 2019

Journal of Experimental Medicine

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The RNase Regnase-1 is a master RNA regulator in macrophages and T cells that degrades cellular and viral RNA upon NF-κB signaling. The roles of its family members, however, remain largely unknown. Here, we analyzed Regnase-3–deficient mice, which develop hypertrophic lymph nodes. We used various mice with immune cell–specific deletions of Regnase-3 to demonstrate that Regnase-3 acts specifically within myeloid cells. Regnase-3 deficiency systemically increased IFN signaling, which increased the proportion of immature B and innate immune cells, and suppressed follicle and germinal center formation. Expression analysis revealed that Regnase-3 and Regnase-1 share protein degradation pathways. Unlike Regnase-1, Regnase-3 expression is high specifically in macrophages and is transcriptionally controlled by IFN signaling. Although direct targets in macrophages remain unknown, Regnase-3 can bind, degrade, and regulate mRNAs, such as Zc3h12a (Regnase-1), in vitro. These data indicate that Regnase-3, like Regnase-1, is an RNase essential for immune homeostasis but has diverged as key regulator in the IFN pathway in macrophages.

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“…PFDL can interact with another chaperone protein (like R2TP), to form an R2TP/PFDL complex, also named PAQosome, a 12-subunit chaperone protein [ 81 ]. Among them, the subunit compositions of R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) is different in yeast and humans [ 82 ]. PAQosome also contains two attachments, Monad/WDR92 and RPB5/POLR2E (Fig.…”

Section: The Multiple Roles Of Prefoldin Subunitsmentioning

confidence: 99%

The functions and mechanisms of prefoldin complex and prefoldin-subunits

et al. 2020

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The correct folding is a key process for a protein to acquire its functional structure and conformation. Prefoldin is a well-known chaperone protein that regulates the correct folding of proteins. Prefoldin plays a crucial role in the pathogenesis of common neurodegenerative diseases (Alzheimer's disease, Parkinson's disease, and Huntington's disease). The important role of prefoldin in emerging fields (such as nanoparticles, biomaterials) and tumors has attracted widespread attention. Also, each of the prefoldin subunits has different and independent functions from the prefoldin complex. It has abnormal expression in different tumors and plays an important role in tumorigenesis and development, especially c-Myc binding protein MM-1. MM-1 can inhibit the activity of c-Myc through various mechanisms to regulate tumor growth. Therefore, an in-depth analysis of the complex functions of prefoldin and their subunits is helpful to understand the mechanisms of protein misfolding and the pathogenesis of diseases caused by misfolded aggregation.

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Immune Responses – Transcriptional and Post-Transcriptional Networks Pass the Baton

Cited by 6 publications

References 13 publications

Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel

Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel

Immune homeostasis and regulation of the interferon pathway require myeloid-derived Regnase-3

The functions and mechanisms of prefoldin complex and prefoldin-subunits

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