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Dynamic molecular architecture of the synaptonemal complex.
Sci Adv
January 2025
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA.
During meiosis, pairing between homologous chromosomes is stabilized by the assembly of the synaptonemal complex (SC). The SC ensures the formation of crossovers between homologous chromosomes and regulates their distribution. However, how the SC regulates crossover formation remains elusive.
View Article and Find Full Text PDFPreventing inappropriate signals pre- and post-ligand perception by a toggle switch mechanism of ERECTA.
Proc Natl Acad Sci U S A
January 2025
HHMI, The University of Texas at Austin, Austin, TX 78712.
Dynamic control of signaling events requires swift regulation of receptors at an active state. By focusing on the Arabidopsis ERECTA (ER) receptor kinase, which perceives peptide ligands to control multiple developmental processes, we report a mechanism preventing inappropriate receptor activity. The ER C-terminal tail (ER_CT) functions as an autoinhibitory domain: Its removal confers higher kinase activity and hyperactivity during inflorescence and stomatal development.
View Article and Find Full Text PDFHijacking of plasminogen by dengue virus: The kringle-4 and -5 domains of plasminogen binds synergistically to the domain I of envelope protein.
Protein Sci
February 2025
Department of Biological Sciences, National University of Singapore, Singapore.
Dengue fever is a serious health issue, particularly in tropical countries like Singapore. We have previously found that dengue virus (DENV) recruits human plasmin in blood meal to enhance the permeability of the mosquito midgut for infection. Here, using biolayer interferometry, we found that neither kringle-4 nor kringle-5 plasmin domains alone binds well to dengue virus.
View Article and Find Full Text PDFNuclear Condensates of WW Domain-Containing Adaptor With Coiled-Coil Regulate Mitophagy via Alternative Splicing.
Adv Sci (Weinh)
January 2025
State Key Laboratory of Oral Diseases and National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, 610041, China.
Biomolecular condensates segregate nuclei into discrete regions, facilitating the execution of distinct biological functions. Here, it is identified that the WW domain containing adaptor with coiled-coil (WAC) is localized to nuclear speckles via its WW domain and plays a pivotal role in regulating alternative splicing through the formation of biomolecular condensates via its C-terminal coiled-coil (CC) domain. WAC acts as a scaffold protein and facilitates the integration of RNA-binding motif 12 (RBM12) into nuclear speckles, where RBM12 potentially interacts with the spliceosomal U5 small nuclear ribonucleoprotein (snRNP).
View Article and Find Full Text PDFStructural mechanism underlying PHO1;H1-mediated phosphate transport in Arabidopsis.
Nat Plants
January 2025
National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.
Arabidopsis PHOSPHATE 1 (AtPHO1) and its closest homologue AtPHO1;H1 are phosphate transporters that load phosphate into the xylem vessel for root-to-shoot translocation. AtPHO1 and AtPHO1;H1 are prototypical members of the unique SPX-EXS family, whose structural and molecular mechanisms remain elusive. In this study, we determined the cryogenic electron microscopy structure of AtPHO1;H1 binding with inorganic phosphate (Pi) and inositol hexakisphosphate in a closed conformation.
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