bioRxiv Science⌕ Search

bioRxiv · 10.1101/2023.07.04.547624

ANGPTL8 R59W variant influences inflammation through modulating NF-κB pathway under TNFα stimulation

Abstract

BackgroundANGPTL8 is known to regulate lipid metabolism and inflammation. It interacts with ANGPTL3 and ANGPTL4 to regulate LPL activity, and with IKK/{beta} to modulate NF-{kappa}B activity. Further, a SNP leading to ANGPTL8 R59W variant associates with reduced LDL/HDL and increased FBG in Hispanic and Arab individuals, respectively. In this study, we investigate the impact of R59W variant on the inflammatory activity of ANGPTL8. MethodsANGPTL8 R59W variant was genotyped in a discovery cohort of 867 Arab individuals from Kuwait. Plasma levels of ANGPTL8 and inflammatory markers were measured and tested for associations with the genotype; the associations were tested for replication in an independent cohort of 278 Arab individuals. Impact of the ANGPTL8 R59W variant on NF-{kappa}B activity was examined using approaches including overexpression, luciferase assay, and structural modeling of binding dynamics. ResultsThe ANGPTL8 R59W variant was associated with increased circulatory levels of TNF and IL7. NF-{kappa}B activity, as assessed by the increased in the phosphorylation of IKK-/{beta} protein, I{kappa}B, and NF-{kappa}B p-65 in R59W variant compared to wild type, and TNF stimulation further elevated it. This finding was substantiated by increased luciferase activity of NF-{kappa}B p65 with the R59W variant. Modeled structural and binding variation due to R59W change in ANGPTL8 agreed with the observed increase in NF-{kappa}B activity. ConclusionANGPTL8 R59W is associated with increased circulatory TNF, IL7 and NF-{kappa}B p65 activity. Weak transient binding of ANGPTL8 R59W variant explains its regulatory role on the NF-{kappa}B pathway and inflammation.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Abu-Farha, M., Madhu, D., Hebbar, P., Mohammad, A., Channanath, A., Kavalakatt, S., Alam-Eldin, N., Alterki, F., Taher, I., Alsmadi, O., Shehab, M., Arefanian, H., Ahmad, R., Al-Mulla, F., Thanaraj, T. A., Abubaker, J.. 2023-07-04. ANGPTL8 R59W variant influences inflammation through modulating NF-κB pathway under TNFα stimulation. https://doi.org/10.1101/2023.07.04.547624

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

EngA adopts multiple distinct conformational states during ribosome assembly

Ribosome assembly, a highly coordinated and crucial cellular process, is assisted by various assembly factors, including GTPases. EngA, an essential P-loop GTPase, is involved in late-stage assembly of the 50S ribosomal subunit. The structures of 50S ribosome in complex with EngA-bound GMPPNP, and EngA-bound GDP alone, without 50S subunit, have been reported previously. However, the molecular mechanism of EngA GTP hydrolysis-assisted 50S maturation remains poorly understood, and structures of the 50S ribosome in complex with EngA-bound GDP have yet to be deciphered. We have reported cryo- EM structures of the Mycobacterium smegmatis 50S ribosome in complex with EngA-bound GTP{gamma}S or GDP at 2.8 - 3.5 [A] resolution. Structural analysis revealed that EngA and 50S subunit undergo a coordinated structural rearrangement, and an assembly intermediate is formed in which the stem-loop of H80 makes base-pair interactions with the junction of H89 and H90, forming a unique stem-loop-junction (SLJ) motif. EngA-bound GDP adopts distinctly different conformations in its ribosome-bound and unbound states. In summary, this study proposed a multi-state conformational model for EngA-assisted ribosome assembly.

biochemistry↗

Modular assembly of mitochondrial complex III from a dynamic matrix domain pool

Mitochondrial complex III is a central component of the cellular energy metabolism. It is an obligate dimer of catalytic and accessory subunits that are encoded by two genomes. How its large matrix domain, formed by the core proteins Qcr1 and Qcr2, is built and joined to the membrane part and during assembly is not known. Here we show that Qcr1 and Qcr2 preassemble independently of complex III into matrix domain modules. Cryo-EM structures from a cardiolipin-deficient yeast strain and of recombinant protein resolved single, double and triple matrix domains, which are linked by the C-terminal tail of Qcr1. In the mature complex III, the same tail binds cytochrome b and cardiolipin. The modules form a dynamic pool, in which assembly species interconvert and exchange subunits. Mutations at the module interfaces, including mimics of human disease variants, reshape this pool and deletion of the Qcr1 tail impairs respiratory growth. Substitution of a tyrosine residue linked to parkinsonism exposes a conserved cysteine residue to oxidation. A cryo-EM structure of an assembly intermediate shows a cap of two matrix domains bound to a monomeric membrane module of cytochrome b, Qcr7, Qcr8 and cytochrome c1. We propose that complex III receives its matrix domain from a dynamic pool of prebuilt modules, which organizes the dimerization of the complex.

biochemistry↗

Vasopressin V2 receptor phosphopeptide reshapes the conformational landscape of arrestin-2 beyond C-tail detachment

Binding of phosphorylated GPCR tails influences arrestin conformation, but the contribution of this interaction to the interdomain rotation associated with activation remains incompletely characterised. In particular, it remains unclear whether displacement of the arrestin C-tail is sufficient to favor larger interdomain rotations or whether the bound phosphotail exerts an additional effect on the conformational landscape. Here, we used enhanced-sampling simulations to characterise the conformational free-energy landscapes of basal (unbound) and V2Rpp-bound arrestin-2. We find that V2Rpp binding broadened the range of energetically accessible interdomain rotation angles relative to basal arrestin-2. However, the pronounced rotation observed in the experimental structures, while accessible, was not strongly favored. Strikingly, C-tail displacement alone does not reproduce this effect, as arrestin-2 retains a strong preference for small interdomain rotation angles in the absence of V2Rpp. Moreover, the C-tail-detached state is energetically unfavorable in the absence of V2Rpp. Together, these findings quantify the effects of V2Rpp binding on the interdomain rotation of arrestin-2 and disentangle the effects of phosphopeptide binding from those of C-tail detachment.

biochemistry↗