Biology subjects

Langin, G.

Publications and source records attributed to Langin, G..

5 recordsLinked to original sources

bioRxiv2026

Gene repertoire expansion and cis-regulatory diversification shaped 26S proteasome evolution within a proteostasis-centered network

The 26S proteasome is essential for proteostasis and constitutes one of the most conserved molecular machineries in eukaryotes. Its homeostasis is maintained by a mechanistically conserved feedback loop involving kingdom-specific components. Yet, how the proteasome subunits and associated regulatory feedback loop have evolved to accommodate ever-changing cellular context is poorly understood. Here, we combine gene duplicate analysis, cis-regulatory element identification, functional validation, and protein network inference to investigate the evolution of plant 26S proteasome. Proteasome gene repertoires expanded largely independently across plant lineages, with paralogs showing shifts in post-translational modification sites and pronounced transcriptional divergence in response to environmental cues. Comparative analysis of 26S proteasome gene promoters revealed extensive diversification of proteasome-associated cis-elements across plants, with repeated enrichment of related motifs. These observations led to the identification of telomere repeat-binding proteins (TRBs) as novel transcriptional regulators of proteasome genes in A. thaliana, through association with the previously characterized PRCE motif. Finally, evolutionary rate covariation analysis identified a conserved proteasome-associated network connected through proteasome-associated cis-elements and unifying cellular proteostasis. Together, our results indicate that plant 26S proteasome is controlled by a regulatory architecture that combines conserved cis-regulatory mechanisms, lineage-specific innovation, and stress-responsive paralog specialization at the center of the proteostasis network; offering a new perspective on the evolution of one of the most essential molecular complexes.

plant biology↗

bioRxiv2026

Autophagy acts as a spatial organizer of cell-type-specific plant immunity

Effective plant immunity requires precise spatial coordination of immune responses across cell-types to restrict pathogens while preventing tissue damage, yet the intracellular pathways that organize this spatial architecture remain unknown. Here we show that autophagy serves as a spatial coordinator of immunity, partitioning and calibrating immune strategies across tissues during Pseudomonas syringae infection in Arabidopsis thaliana. Combining single-cell transcriptomics, cell-type-specific complementation, and live-cell imaging, we uncover distinct and opposing roles of autophagy across tissues. In guard cells, autophagy promotes pathogen-induced stomatal reopening by suppressing abscisic acid (ABA) signalling in part via autophagic turnover of the guard cell ABA receptor PYL4. In contrast, in mesophyll cells, autophagy restricts immune activation while simultaneously enabling effective immune execution: its loss enhances EDS1-PAD4-ADR1 pathway expression yet compromises PTI outputs. Mechanistically, bacterial infection triggers autophagic EDS1 turnover, supporting a model in which controlled EDS1 recycling facilitates HR elicitation. Cell-type-specific complementation reveals that PTI competence may involve coordinated autophagy across tissues, whereas mesophyll-autonomous autophagy is partially sufficient for HR execution. Together, these findings establish a framework in which spatial control of proteostasis orchestrates multicellular immune coordination, with broad implications for understanding how conserved degradation pathways regulate layered immunity across organisms.

plant biology↗

bioRxiv2025

Effector-triggered processing body formation attenuates host translation via ER stress responses and autophagy upon bacterial infection

Pathogens employ sophisticated strategies to modulate host protein homeostasis by targeting proteolytic pathways, but their impact on protein synthesis remains elusive. We report that pathogenic bacteria Pseudomonas syringae (Pst) targets ribonucleoprotein condensates, known as processing bodies (P-bodies), to attenuate host translation through two effectors with liquid-like properties. We uncovered a previously unknown link that Pst-mediated repression of the ER stress response is required for P-body assembly. Furthermore, we identify a novel intersection between P-bodies and autophagy, demonstrating that autophagic clearance of P-bodies is crucial for maintaining the balance between translationally active and inactive mRNAs. Altogether, our discoveries provide novel insights on how host translation is attenuated by bacteria to dampen plant immunity and uncover unknown connections between ER stress responses and autophagy with P-body dynamics.

plant biology↗

bioRxiv2023

ER-anchored protein sorting controls the fate of two proteasome activators for intracellular organelle communication during proteotoxic stress

Proteotoxic stress, characterized by the accumulation of damaged proteins, poses a significant challenge to cellular homeostasis. To mitigate proteotoxicity eukaryotes employ the proteasome that is regulated by proteasome activators, e.g. transcription factors that promote gene expression of proteasome subunits. As proteotoxicity originates in different compartments, cells need to perceive signals from various locations. Understanding which components integrate signals to address proteotoxicity is essential to develop strategies to cope with proteotoxicity but remain elusive. Here, we identify that the proteasome autoregulatory feedback loop acts as a gatekeeper to facilitate the communication between nucleus and chloroplast. We reveal that the ER-anchored protein sorting system (ERAPS) controls the proteasomal degradation or nuclear translocation of proteasome activators NAC53 and NAC78. While both transcription factors activate the proteasome gene expression, they repress photosynthesis-associated nuclear genes during proteotoxicity through association with a conserved cis-element. Our data implicate a general trade-off between proteasome function and energy metabolism unravelling an unprecedented mechanism of how eukaryotic cells cope with proteotoxicity. Collectively, our discoveries provide a novel conceptual framework in which the proteasome autoregulatory feedback loop coordinates subcellular proteostasis and the trade-off between growth and defence.

plant biology↗

bioRxiv2021

Self-ubiquitination of a pathogen type-III effector traps and blocks the autophagy machinery to promote disease

Beyond its role in cellular homeostasis, autophagy plays anti- and pro-microbial roles in host-microbe interactions, both in animals and plants. One prominent role of anti-microbial autophagy is to degrade intracellular pathogens or microbial molecules, in a process termed xenophagy. Consequently, microbes evolved mechanisms to hijack or modulate autophagy to escape elimination. Although well-described in animals, the extent to which xenophagy contributes to plant-bacteria interactions remains unknown. Here, we provide evidence that Xanthomonas campestris pv. vesicatoria (Xcv) suppresses host autophagy by utilizing type-III effector XopL. XopL interacts with and degrades the autophagy component SH3P2 via its E3 ligase activity to promote infection. Intriguingly, XopL is targeted for degradation by defense-related selective autophagy mediated by NBR1/Joka2, revealing a complex antagonistic interplay between XopL and the host autophagy machinery. Our results implicate plant antimicrobial autophagy in depletion of a bacterial virulence factor and unravels an unprecedented pathogen strategy to counteract defense-related autophagy.

plant biology↗