ArticlePloS one2009
Pyrin Modulates the Intracellular Distribution of PSTPIP1.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- Recent Insights in Pyrin Inflammasome Activation: Identifying Potential Novel Therapeutic Approaches in Pyrin-Associated Autoinflammatory Syndromes.Journal of clinical immunology · 2023Review
- IL-1 and autoinflammatory disease: biology, pathogenesis and therapeutic targeting.Nature reviews. Rheumatology · 2022Review
- Immune-mediated inflammatory diseases with chronic excess of serum interleukin-18.Frontiers in immunology · 2022Review
- The Genomic Architecture of Hidradenitis Suppurativa-A Systematic Review.Frontiers in genetics · 2022Review
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- Moving towards a systems-based classification of innate immune-mediated diseases.Nature reviews. Rheumatology · 2020Review
- Ancient friends, revisited: Systematic review and case report of pyoderma gangrenosum-associated autoinflammatory syndromes.Journal of translational autoimmunity · 2020Review
- Current and future advances in genetic testing in systemic autoinflammatory diseases.Rheumatology (Oxford, England) · 2019Review
- Inflammasome-Dependent Cytokines at the Crossroads of Health and Autoinflammatory Disease.Cold Spring Harbor perspectives in biology · 2019Review
- The Pyrin Inflammasome in Health and Disease.Frontiers in immunology · 2019Review
- A novel Pyrin-Associated Autoinflammation with Neutrophilic Dermatosis mutation further defines 14-3-3 binding of pyrin and distinction to Familial Mediterranean Fever.Annals of the rheumatic diseases · 2017Article
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
- Single amino acid charge switch defines clinically distinct proline-serine-threonine phosphatase-interacting protein 1 (PSTPIP1)-associated inflammatory diseases.The Journal of allergy and clinical immunology · 2015Article
- The F-BAR protein PSTPIP1 controls extracellular matrix degradation and filopodia formation in macrophages.Blood · 2014Article
- Autoinflammatory bone disorders with special focus on chronic recurrent multifocal osteomyelitis (CRMO).Pediatric rheumatology online journal · 2013Article
- Autoinflammatory pustular neutrophilic diseases.Dermatologic clinics · 2013Review
- [Uncommon acne-associated syndromes and their significance in understanding the pathogenesis of acne].Der Hautarzt; Zeitschrift fur Dermatologie, Venerologie, und verwandte Gebiete · 2013Article
- Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization.Immunity · 2012Article
- Brief report: genotype, phenotype, and clinical course in five patients with PAPA syndrome (pyogenic sterile arthritis, pyoderma gangrenosum, and acne).Arthritis and rheumatism · 2012Article
- Clinical, Molecular, and Genetic Characteristics of PAPA Syndrome: A Review.Current genomics · 2010Article
Corrections and comments
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Authors and funding
12 authors at 7 institutions in 3 countries.
Funding
Abstract
PSTPIP1 is a cytoskeleton-associated adaptor protein that links PEST-type phosphatases to their substrates. Mutations in PSTPIP1 cause PAPA syndrome (Pyogenic sterile Arthritis, Pyoderma gangrenosum, and Acne), an autoinflammatory disease. PSTPIP1 binds to pyrin and mutations in pyrin result in familial Mediterranean fever (FMF), a related autoinflammatory disorder. Since disease-associated mutations in PSTPIP1 enhance pyrin binding, PAPA syndrome and FMF are thought to share a common pathoetiology. The studies outlined here describe several new aspects of PSTPIP1 and pyrin biology. We document that PSTPIP1, which has homology to membrane-deforming BAR proteins, forms homodimers and generates membrane-associated filaments in native and transfected cells. An extended FCH (Fes-Cip4 homology) domain in PSTPIP1 is necessary and sufficient for its self-aggregation. We further show that the PSTPIP1 filament network is dependent upon an intact tubulin cytoskeleton and that the distribution of this network can be modulated by pyrin, indicating that this is a dynamic structure. Finally, we demonstrate that pyrin can recruit PSTPIP1 into aggregations (specks) of ASC, another pyrin binding protein. ASC specks are associated with inflammasome activity. PSTPIP1 molecules with PAPA-associated mutations are recruited by pyrin to ASC specks with particularly high efficiency, suggesting a unique mechanism underlying the robust inflammatory phenotype of PAPA syndrome.
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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.