Biology subjects

Potel, C.

Publications and source records attributed to Potel, C..

3 recordsLinked to original sources

bioRxiv2023

Molecular profiling of sponge deflation reveals an ancient relaxant-inflammatory response

A hallmark of animals is the coordination of whole-body movement. Neurons and muscles are central to this, yet coordinated movements also exist in sponges that lack these cell types. Sponges are sessile animals with a complex canal system for filter-feeding. They undergo whole-body movements resembling "contractions" that lead to canal closure and water expulsion. Here, we combine 3D optical coherence microscopy, pharmacology, and functional proteomics to elucidate anatomy, molecular physiology, and control of these movements. We find them driven by the relaxation of actomyosin stress fibers in epithelial canal cells, which leads to whole-body deflation via collapse of the incurrent and expansion of the excurrent system, controlled by an Akt/NO/PKG/A pathway. A concomitant increase in reactive oxygen species and secretion of proteinases and cytokines indicate an inflammation-like state reminiscent of vascular endothelial cells experiencing oscillatory shear stress. This suggests an ancient relaxant-inflammatory response of perturbed fluid-carrying systems in animals. HighlightsO_LISponge deflation is driven by tension release in actomyosin stress fibers of epithelial pinacocytes C_LIO_LIAkt kinase/Nitric oxide/Protein kinase G/A regulate actomyosin relaxation C_LIO_LIAgitation-induced deflation coincides with an inflammatory state C_LIO_LIThe sponge relaxant-inflammatory response is evolutionary related to similar responses in the vertebrate vascular system C_LI

molecular biology↗

bioRxiv2022

Nudibranch predation boosts sponge silicon cycling

Sponges are singular players in the marine silicon cycle. They accumulate vast stocks of biogenic silica within their bodies and in the sediments beneath them over long periods. These silica stocks are recycled at slow rates, much slower than that of other silicon users such as diatoms. The observation of an abrupt change in sponge biomass in a temperate coastal ecosystem led us to study the effect of nudibranch (Doris verrucosa) predation on the silicon budget of a sponge (Hymeniacidon perlevis) population on an annual scale. Predation rates and the associated sponge silicon fluxes were determined. After 5 months of predation, the abundance of sponge individuals did not change but their biomass decreased by 95%, of which 48% can be explained by nudibranch predation. About 97% of sponge spicules ingested by nudibranchs while feeding was excreted, most of them unbroken, implying a high rate of sponge silica deposition in the surrounding sediments. After predation, sponges partially recovered their biomass stocks within 7 months. This involved a rapid growth rate and large consumption of dissolved silicon, with the highest rates ever recorded unexpectedly occurring when the dissolved silicon concentration was minimal in seawater (< 1.5 M). These findings reveal that the annual sponge predation-recovery cycle triggers unprecedented intra-annual changes in sponge silicon stocks and boosts nutrient cycling. They also highlight the need for intra-annual data collection to understand the dynamics and resilience of sponge ecosystem functioning.

ecology↗

bioRxiv2022

Protein-Peptide Turnover Profiling reveals wiring of phosphorylation during protein maturation

Post-translational modifications (PTMs) regulate various aspects of protein function, including degradation. Mass spectrometric methods that rely on pulsed metabolic labeling are very popular to quantify turnover rates on a proteome-wide scale. Such data have often been interpreted in the context of protein proteolytic stability. Here, we combine theoretical kinetic modeling with experimental pulsed stable isotope labeling of amino acids in cell culture (pSILAC) for the study of protein phosphorylation. We demonstrate that metabolic labeling combined with PTM-specific enrichment does not measure effects of PTMs on protein stability. Rather, it reveals the relative order of PTM addition and removal along a proteins lifetime--a fundamentally different metric. We use this framework to identify temporal phosphorylation sites on cell cycle-specific factors and protein complex assembly intermediates. Our results open up an entirely new aspect in the study of PTMs, by tying them into the context of a proteins lifetime.

biochemistry↗