ArticleThe Journal of biological chemistry2014
Zymogen activation and subcellular activity of subtilisin kexin isozyme 1/site 1 protease.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- SPRINGing off the lock: the role of SPRING in S1P activity and SREBP-regulated lipid metabolism.Current opinion in lipidology · 2025Review
- Structural basis for substrate selectivity by site-one protease revealed by studies with a small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SPRING licenses S1P-mediated cleavage of SREBP2 by displacing an inhibitory pro-domain.Nature communications · 2024Article
- SPRING is a Dedicated Licensing Factor for SREBP-Specific Activation by S1P.Molecular and cellular biology · 2024Article
- Caspase-11 contributes to site-1 protease cleavage and SREBP1 activation in the inflammatory response of macrophages.Frontiers in immunology · 2023Article
- How Do Enveloped Viruses Exploit the Secretory Proprotein Convertases to Regulate Infectivity and Spread?Viruses · 2021Review
- POST1/C12ORF49 regulates the SREBP pathway by promoting site-1 protease maturation.Protein & cell · 2021Article
- Article
- The PCSK9 revolution and the potential of PCSK9-based therapies to reduce LDL-cholesterol.Global cardiology science & practice · 2017Review
- Structure-function relationship of the mammarenavirus envelope glycoprotein.Virologica Sinica · 2016Review
- Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P).The Journal of biological chemistry · 2016Article
- A Molecular Sensor To Characterize Arenavirus Envelope Glycoprotein Cleavage by Subtilisin Kexin Isozyme 1/Site 1 Protease.Journal of virology · 2016Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
The proprotein convertase subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P) plays crucial roles in cellular homeostatic functions and is hijacked by pathogenic viruses for the processing of their envelope glycoproteins. Zymogen activation of SKI-1/S1P involves sequential autocatalytic processing of its N-terminal prodomain at sites B'/B followed by the herein newly identified C'/C sites. We found that SKI-1/S1P autoprocessing results in intermediates whose catalytic domain remains associated with prodomain fragments of different lengths. In contrast to other zymogen proprotein convertases, all incompletely matured intermediates of SKI-1/S1P showed full catalytic activity toward cellular substrates, whereas optimal cleavage of viral glycoproteins depended on B'/B processing. Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments. Using a cell-based sensor for SKI-1/S1P activity, we found that 9 amino acid residues at the cleavage site (P1-P8) and P1' are necessary and sufficient to define the subcellular location of processing and to determine to what extent processing of a substrate depends on SKI-1/S1P maturation. In sum, our study reveals novel and unexpected features of SKI-1/S1P zymogen activation and subcellular specificity of activity toward cellular and pathogen-derived substrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.