Biology subjects

Lauth, M.

Publications and source records attributed to Lauth, M..

3 recordsLinked to original sources

bioRxiv2026

Life inside polymetallic nodules

Deep-sea abyssal plains harbour extensive biodiversity, much of which remains undocumented. Polymetallic nodules in the abyssal plains of the Clarion-Clipperton Zone (CCZ), Central Pacific, harbour diverse meiofaunal communities within their crevices, representing an understudied habitat. Given their high concentrations of nickel, copper, and cobalt, nodules are currently one of the primary targets for the extraction of deep-sea mineral resources. Here, we characterise the physical properties of polymetallic nodules, quantify their meiofaunal crevice communities, and compare them to those from the nearby sediments. We show that nodules contain internal cracks and microfossils, that their crevices harbour meiofaunal communities dominated by nematodes and copepods, and that faunal abundance increases significantly with nodule volume. Nodule-crevice nematode and copepod abundances were equivalent to approximately 10% and 25%, respectively, of those recorded in nearby sediments across the two exploration contract areas in the eastern CCZ. Based on 18S rRNA data, nematode and copepod assemblages recovered from nodule crevices differed from those recovered from nearby sediments collected during the same expedition and within the same exploration contract areas. Our findings, therefore, point to the possibility of nodule-associated crevice meiofauna communities and the consequent risk of biodiversity loss associated with nodule removal through potential future commercial mining.

ecology↗

bioRxiv2026

Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodies

Dual-specificity tyrosine-phosphorylation-regulated kinase 1B (DYRK1B) modulates the cell cycle, cell fate during development, and is deregulated in cancer and metabolic syndrome. However, only a few DYRK1B substrates have been defined, so we undertook a phosphoproteomics screen in cells that exhibit inducible DYRK1B expression. Motif analysis revealed enrichment for proline-directed serine or threonine phosphorylation sites (pSer/pThr-Pro), consistent with the consensus motif of class I DYRKs. Gene ontology analysis revealed enrichment of proteins involved in mRNA binding, mRNA processing and ribonucleoprotein complexes. Several processing body (PB) components, including DCP1A, PATL1(PAT1B), EDC3 and 4E-T, were identified as DYRK1B-inducible phosphoproteins. DYRK1B also co-immunoprecipitated with DCP1A, PAT1B, EDC3, EDC4, DDX6 and XRN1. Super-resolution microscopy demonstrated that DYRK1B co-localised with DCP1A, DCP1B and DDX6 in PBs. Activation of DYRK1B increased PB abundance, whereas inhibition, depletion or knockout of DYRK1B reduced phosphorylation of DCP1A and 4E-T and decreased PB number. Re-expression of wild type, but not kinase-dead, DYRK1B restored PB numbers in knockout cells. These findings reveal novel DYRK1B targets and establish DYRK1B as a regulator of processing body abundance. HighlightsO_LIDYRK1B induces phosphorylation of a cluster of RNA binding and processing body associated proteins. C_LIO_LIDYRK1B localises to PBs and associates with multiple PB components. C_LIO_LIDYRK1B controls P-body abundance in a kinase-dependent manner. C_LI

cell biology↗

bioRxiv2026

Tumor Cell Death Drives Tumor-Promoting IL-6+ iCAF formation via P2X7-activation

Chemotherapy resistance in pancreatic ductal adenocarcinoma is commonly attributed to tumor cell-intrinsic mechanisms, yet how cytotoxic therapy reshapes the tumor microenvironment remains incompletely understood. Here we show that PDAC cells exposed to cytotoxic agents reprogram pancreatic stellate cells toward an inflammatory cancer-associated fibroblast phenotype. Mechanistically, chemotherapy triggers the release of ATP from dying PDAC cells, which activates P2X7 signaling in PSCs in a paracrine manner, leading ERK activation and inflammatory polarization. In turn, therapy-educated PSCs promote tumor cell proliferation, induce resistance-associated transcriptional programs and impair CD8 T cell-mediated cytotoxicity in an IL-6-dependent manner. Pharmacological inhibition of P2X7 suppressed stromal IL-6 induction and enhanced gemcitabine efficacy in vivo. These findings identify a therapy-induced ATP-P2X7-IL-6 axis that links tumor cell death to stromal reprogramming and adaptive resistance in PDAC.

cancer biology↗