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Introduction: Rice, a cornerstone of global food security, faces escalating demands for enhanced yield and disease resistance. We collected 300 high-quality genomes, representing both cultivated (, , and ) and wild species (, , and ).
Methods: Leveraging HMMER, NLR-Annotator, and OrthoFinder, we systematically identified 148,077 leucine-rich repeat (LRR) and 143,459 nucleotide-binding leucine-rich repeat (NLR) genes, with LRR receptor-like kinases (LRR-RLKs) dominating immune receptor proportions, followed by coiled-coil domain containing (CNL)-type NLRs and LRR receptor-like proteins (LRR-RLPs).
Results: Benchmarking Universal Single-Copy Orthologs (BUSCO) assessments confirmed robust genome quality (average score: 94.78). Strikingly, 454 TIR-NB-LRR (TNL) genes-typically rare in monocots-were detected, challenging prior assumptions. Phylogenetic analysis with Arabidopsis TNLs highlighted five genes clustering with dicot TNLs; these genes featured truncated PLN03210 motifs fused to nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4 (NB-ARC) and LRR domains.
Conclusions: By bridging structural genomics, evolutionary dynamics, and domestication-driven adaptation, this work provides a foundation for targeted breeding strategies and advances functional studies of plant immunity in rice.
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http://dx.doi.org/10.3390/genes16050597 | DOI Listing |
J Biol Chem
September 2025
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, United States; Aligning Science Across Parkinson's (ASAP) Collaborative Research Network, San Francisco, CA, United States. Electronic address:
PPM1H phosphatase reverses Parkinson's disease-associated, Leucine Rich Repeat Kinase 2-mediated, Rab GTPase phosphorylation. We showed previously that PPM1H relies on an N-terminal amphipathic helix for Golgi membrane localization and this helix enables PPM1H to associate with liposomes in vitro; binding to highly curved liposomes activates PPM1H's phosphatase activity. We show here that PPM1H also contains an allosteric binding site for its non-phosphorylated reaction products, Rab8A and Rab10.
View Article and Find Full Text PDFThe end-stage pathology of Parkinson's disease (PD) involves the loss of dopamine-producing neurons in the substantia nigra pars compacta (SNc). However, synaptic deregulation of these neurons begins much earlier. Understanding the mechanisms behind synaptic deficits is crucial for early therapeutic intervention, yet these remain largely unknown.
View Article and Find Full Text PDFVolume-regulated anion channels (VRACs) are large-pore channels present in nearly all vertebrate cells, playing key roles in cell volume regulation and autocrine/paracrine signaling. Here, we identify the ubiquitously expressed puromycin-sensitive aminopeptidase (PSA) as a binding partner of the obligatory VRAC subunit SWELL1 (also known as LRRC8A) and report the cryo-electron microscopy structure of the SWELL1-PSA complex. Three PSA molecules associate with a single SWELL1 hexamer, coupling adjacent leucine-rich repeat (LRR) domains into local dimers.
View Article and Find Full Text PDFMol Plant
September 2025
Zhejiang Provincial Key Laboratory of Agricultural Microbiomics, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China. Electronic address:
Effector-triggered immunity (ETI) in plants is mediated by intracellular nucleotide-binding leucine-rich repeat receptors (NLRs), which converge on calcium (Ca) signaling pathways. However, how NLR-induced Ca signals initiate downstream immune responses, such as enhancing reactive oxygen species (ROS) signaling, remains largely unclear. In this study, we identified a calcium-dependent protein kinase (CPK) that regulates sustained ETI-ROS signaling.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, Korea. Electronic address:
Leucine-rich repeat kinase 2 (LRRK2), a large protein with kinase and GTPase activities, regulates various cellular pathways, including autophagy, endocytosis, and mitochondrial dynamics. LRRK2, extensively studied in the context of Parkinson's disease, is functionally impaired in other pathological conditions as well, including inflammatory bowel disease, cancer, and cardiovascular diseases. Despite its critical functions, the mechanisms controlling LRRK2 protein stability are not fully understood.
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