ArticleNature communications2023
A signal peptide peptidase is required for ER-symbiosome proximal association and protein secretion.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- A Simplified Density Gradient-Free Method for Isolating Functional Symbiosomes From Legume Nodules.Bio-protocol · 2026Article
- ESN3, a nodule-specific small peptide essential for symbiotic nitrogen fixation in Medicago truncatula.The New phytologist · 2026Article
- Genomic and Functional Characterization of the EndophyticMicroorganisms · 2026Article
- Signal peptide peptidase-like proteases OsSPPL1 and OsSPPL2 facilitate ER-associated protein degradation in rice.Nature communications · 2026Article
- Identification and functional evaluation of cyclin-dependent kinase genes reveals that CDKB1;1 and CDKB2;2 contribute to the balance of mitosis and endoreduplication in Medicago truncatula nodule.BMC plant biology · 2025Article
- Article
- The symbiosome-a transient organelle in evolution.Journal of experimental botany · 2024Article
- Signal Peptide Peptidase and PI4Kβ1/2 play opposite roles in plant ER stress response and immunity.Stress biology · 2024Article
- Targeted mutagenesis of Medicago truncatula Nodule-specific Cysteine-Rich (NCR) genes using the Agrobacterium rhizogenes-mediated CRISPR/Cas9 system.Scientific reports · 2023Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During legume-rhizobia symbiosis, differentiation of the symbiosome (engulfed intracellular rhizobia) is necessary for successful nitrogen fixation. To control symbiosome differentiation, host cell subcellular components, e.g., ER (endoplasmic reticulum), must adapt robustly to ensure large-scale host protein secretion to the new organelle. However, the key components controlling the adaption of ER in nodule cells remain elusive. We report that Medicago BID1, a nodule-specific signal peptide peptidase (SPP), is central to ER structural dynamics and host protein secretion. In bid1, symbiosome differentiation is blocked. BID1 localizes specifically to the ER membrane and expresses exclusively in nodule cells with symbiosomes. In the wild type ER forms proximal association structures with symbiosomes, but not in bid1. Consequently, in bid1 excessive ER stress responses are induced and ER-to-symbiosome protein secretion is impaired. In summary, a nodule-specific SPP is necessary for ER-symbiosome proximal association, host protein secretion, and symbiosome differentiation.
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