ArticleProceedings of the National Academy of Sciences of the United States of America2013
Site-2 protease substrate specificity and coupling in trans by a PDZ-substrate adapter protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Close Related Drug-Resistance Beijing Isolates ofInternational journal of molecular sciences · 2022Article
- MBTPS2, a membrane bound protease, underlying several distinct skin and bone disorders.Journal of translational medicine · 2021Review
- In Vivo Methods to Study Protein-Protein Interactions as Key Players inPathogens (Basel, Switzerland) · 2019Review
- Chemical Genetic Interaction Profiling Reveals Determinants of Intrinsic Antibiotic Resistance in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2017Article
- Themes and variations in gene regulation by extracytoplasmic function (ECF) sigma factors.Current opinion in microbiology · 2017Review
- Discrimination and Integration of Stress Signals by Pathogenic Bacteria.Cell host & microbe · 2016Review
- Complex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σK.The Journal of biological chemistry · 2016Article
- The Rip1 protease of Mycobacterium tuberculosis controls the SigD regulon.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Site-2 proteases (S2Ps) are intramembrane metalloproteases that cleave transmembrane substrates in all domains of life. Many S2Ps, including human S2P and Mycobacterium tuberculosis Rip1, have multiple substrates in vivo, which are often transcriptional regulators. However, S2Ps will also cleave transmembrane sequences of nonsubstrate proteins, suggesting additional specificity determinants. Many S2Ps also contain a PDZ domain, the function of which is poorly understood. Here, we identify an M. tuberculosis protein, PDZ-interacting protease regulator 1 (Ppr1), which bridges between the Rip1 PDZ domain and anti-sigma factor M (Anti-SigM), a Rip1 substrate, but not Anti-SigK or Anti-SigL, also Rip1 substrates. In vivo analyses of Ppr1 function indicate that it prevents nonspecific activation of the Rip1 pathway while coupling Rip1 cleavage of Anti-SigM, but not Anti-SigL, to site-1 proteolysis. Our results support a model of S2P substrate specificity in which a substrate-specific adapter protein tethers the S2P to its substrate while holding the protease inactive through its PDZ domain.
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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.