ArticleScientific reports2016
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- LONP1 Variants Are Associated With Clinically Diverse Phenotypes.Clinical genetics · 2026Article
- Role of LONP1 in human diseases: molecular mechanisms and therapeutic potential.Cellular & molecular biology letters · 2026Review
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM Reveals Regulatory Mechanisms Governing Substrate Selection and Activation of Human LONP1.bioRxiv : the preprint server for biology · 2025Article
- Quality control at the powerhouse: mitochondrial proteostasis dysfunction and disease.Biochemical Society transactions · 2025Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.Scientific reports · 2024Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Article
- Roles of LonP1 in Oral-Maxillofacial Developmental Defects and Tumors: A Novel Insight.International journal of molecular sciences · 2022Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.Nature communications · 2021Article
- DNA polymerase gamma mutations that impair holoenzyme stability cause catalytic subunit depletion.Nucleic acids research · 2021Article
- NEK5 interacts with LonP1 and its kinase activity is essential for the regulation of mitochondrial functions and mtDNA maintenance.FEBS open bio · 2021Article
- 'Frontiers in microbiology · 2021Article
- LONP1 de novo dominant mutation causes mitochondrial encephalopathy with loss of LONP1 chaperone activity and excessive LONP1 proteolytic activity.Mitochondrion · 2020Article
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- Crystal structure of the N domain of Lon protease from Mycobacterium avium complex.Protein science : a publication of the Protein Society · 2019Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lon is an essential, multitasking AAA(+) protease regulating many cellular processes in species across all kingdoms of life. Altered expression levels of the human mitochondrial Lon protease (hLon) are linked to serious diseases including myopathies, paraplegia, and cancer. Here, we present the first 3D structure of full-length hLon using cryo-electron microscopy. hLon has a unique three-dimensional structure, in which the proteolytic and ATP-binding domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. These two domains are linked by a narrow trimeric channel composed likely of coiled-coil helices. In the presence of AMP-PNP, the AP-domain has a closed-ring conformation and its N-terminal entry gate appears closed, but in ADP binding, it switches to a lock-washer conformation and its N-terminal gate opens, which is accompanied by a rearrangement of the N-terminal domain. We have also found that both the enzymatic activities and the 3D structure of a hLon mutant lacking the first 156 amino acids are severely disturbed, showing that hLon's N-terminal domains are crucial for the overall structure of the hLon, maintaining a conformation allowing its proper functioning.
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