bioRxiv Science⌕ Search

Biology subjects

Xavier, B.

Publications and source records attributed to Xavier, B..

2 recordsLinked to original sources

Direct interaction between miR-210-5p and HIF-1α regulates HIF-dependent transcription

Hypoxia-inducible factors (HIFs) coordinate cellular adaptation to oxygen deprivation, yet whether hypoxia-induced microRNAs directly regulate HIF-dependent transcription remains unknown. Here, we identify miR-210-5p as a nuclear hypoxamiR that directly binds HIF-1 and enhances HIF-dependent transcription. Hypoxia induced rapid, HIF-dependent nuclear accumulation of mature miR-210-5p across multiple cell types. Biophysical analyses demonstrated direct interaction between miR-210-5p and the HIF-1 bHLH-PAS domain, while mutational studies identified a conserved 5'motif required for HIF-1 binding but dispensable for repression of the canonical cytoplasmic target ISCU. Functionally, transcriptional activity closely correlated with HIF-1-binding affinity, as binding-deficient variants failed to activate HIF reporters or endogenous target genes. Although AGO2 contributed to hypoxic transcriptional responses, miR-210-5p interacted directly with HIF-1 independently of AGO2. In ischemic myocardium, nuclear enrichment of miR-210-5p and its proximity to HIF-1 support the physiological relevance of this mechanism, revealing a previously unrecognized RNA-mediated layer of HIF transcriptional regulation.

molecular biology↗

Mapping the MIF-2 Chemokine Interactome Reveals MIF-2-CCL20 Complex Formation in Liver Fibrosis

D-dopachrome tautomerase (D-DT/MIF-2) is an inflammatory cytokine, atypical chemokine (ACK) and member of the macrophage migration-inhibitory factor (MIF) family. While interactions among classical chemokines (CKs) are established, ACK-CK interactions remain underexplored. Here, we screened for MIF-2 binding-partners using a protein array encompassing all CKs and selected ACKs, and validated candidate interactors by surface-plasmon resonance. CCL20/MIP-3 was prioritized based on RNA-sequencing suggesting induction during liver fibrosis. MIF-2/CCL20 complex formation was verified by microscale thermophoresis and interaction interfaces mapped using peptide array and in-silico modeling. The deduced binding-site near the MIF-2 tautomerase pocket was consistent with inhibition of its tautomerase activity by CCL20. We found both proteins abundantly expressed in human liver tissue, with a positive correlation. Pull-down confirmed complex formation and proximity ligation assay demonstrated MIF-2/CCL20 complexes in liver in situ, with higher levels in fibrotic tissue. Functionally, MIF-2/CCL20 complexes suppressed MIF-2-driven CD4 T-cell chemotaxis and fibroblast IL-6 secretion, indicating modulation of immune and stromal responses. This study extends the ACK interactome to MIF-2 and suggests ACK/CK complexes modulate chemokine activities in liver fibrosis.

immunology↗