ArticleScientific reports2017
Actin-binding protein coronin 1A controls osteoclastic bone resorption by regulating lysosomal secretion of cathepsin K.
Article in Scientific reports, 2017. 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.
- Heparan sulfate promotes autoactivation of procathepsin K by destabilizing the propeptide-catalytic domain interaction.The Biochemical journal · 2026Article
- CORO1A links inflammatory chondrocyte subpopulations to immune microenvironment alterations in osteoarthritis: an integrative multi-omics and single-cell study.Frontiers in immunology · 2026Article
- Cationic Hydroxyethyl Cellulose Nanocomplexes and RANK siRNA/Zoledronate Co-Delivery Systems for Osteoclast Inhibition.Pharmaceutics · 2024Article
- Gene expression in notochord and nuclei pulposi: a study of gene families across the chordate phylum.BMC ecology and evolution · 2023Article
- Overview of multifunctional cysteinyl cathepsins in atherosclerosis-based cardiovascular disease: from insights into molecular functions to clinical implications.Cell & bioscience · 2023Review
- Coronin1C Is a GDP-Specific Rab44 Effector That Controls Osteoclast Formation by Regulating Cell Motility in Macrophages.International journal of molecular sciences · 2022Article
- Differential proteomic analysis of tibial subchondral bone from male and female guinea pigs with spontaneous osteoarthritis.Experimental and therapeutic medicine · 2021Article
- Characterization of New Proteomic Biomarker Candidates in Mucopolysaccharidosis Type IVA.International journal of molecular sciences · 2020Article
- Macrophages Switch to an Osteo-Modulatory Profile Upon RANKL Induction in a Medaka (JBMR plus · 2020Article
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Authors and funding
15 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Osteoclasts degrade bone matrix proteins via the secretion of lysosomal enzymes. However, the precise mechanisms by which lysosomal components are transported and fused to the bone-apposed plasma membrane, termed ruffled border membrane, remain elusive. Here, we identified coronin 1A as a negative regulator of exocytotic release of cathepsin K, one of the most important bone-degrading enzymes in osteoclasts. The modulation of coronin 1A expression did not alter osteoclast differentiation and extracellular acidification, but strongly affected the secretion of cathepsin K and osteoclast bone-resorption activity, suggesting the coronin 1A-mediated regulation of lysosomal trafficking and protease exocytosis. Further analyses suggested that coronin 1A prevented the lipidation-mediated sorting of the autophagy-related protein LC3 to the ruffled border and attenuated lysosome-plasma membrane fusion. In this process, the interactions between coronin 1A and actin were crucial. Collectively, our findings indicate that coronin 1A is a pivotal component that regulates lysosomal fusion and the secretion pathway in osteoclast-lineage cells and may provide a novel therapeutic target for bone diseases.
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