ArticleCellular and molecular life sciences : CMLS2022
PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders.
Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Expression of PSTPIP1 in Renal Cell Carcinoma and Its Prognostic Value.Biochemical genetics · 2026Article
- Autoinflammatory disease and severe neutropenia due toJournal of human immunity · 2026Article
- A protracted diagnostic journey of pediatric PAPA syndrome and subsequent response to tofacitinib therapy: a case report and literature review.Frontiers in immunology · 2026Review
- LYP regulates SLP76 and other adaptor proteins in T cells.Biological research · 2024Article
- Interrupting an IFN-γ-dependent feedback loop in the syndrome of pyogenic arthritis with pyoderma gangrenosum and acne.Annals of the rheumatic diseases · 2024Article
- Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily.Cells · 2024Article
- A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular Signaling.Cells · 2023Review
- Efficacy and safety of anakinra and canakinumab in PSTPIP1-associated inflammatory diseases: a comprehensive scoping review.Frontiers in immunology · 2023Article
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Authors and funding
9 authors.
Funding
Abstract
Mutations in the adaptor protein PSTPIP1 cause a spectrum of autoinflammatory diseases, including PAPA and PAMI; however, the mechanism underlying these diseases remains unknown. Most of these mutations lie in PSTPIP1 F-BAR domain, which binds to LYP, a protein tyrosine phosphatase associated with arthritis and lupus. To shed light on the mechanism by which these mutations generate autoinflammatory disorders, we solved the structure of the F-BAR domain of PSTPIP1 alone and bound to the C-terminal homology segment of LYP, revealing a novel mechanism of recognition of Pro-rich motifs by proteins in which a single LYP molecule binds to the PSTPIP1 F-BAR dimer. The residues R228, D246, E250, and E257 of PSTPIP1 that are mutated in immunological diseases directly interact with LYP. These findings link the disruption of the PSTPIP1/LYP interaction to these diseases, and support a critical role for LYP phosphatase in their pathogenesis.
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