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Updated: Apr 7, 2026

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy
Published on: November 1, 2021
Pyrin-PSTPIP1 colocalises at the leading edge during cell migration
Yeliz Z Akkaya-Ulum1, Banu Balci-Peynircioglu1, Nuhan Purali2
1Department of Medical Biology, Faculty of Medicine, Hacettepe University, Sihhiye, Ankara, 06100, Turkey.
Abstract:
A set of mutations in the MEditerranean FeVer (MEFV) gene causes familial Mediterranean fever (FMF), the most common auto-inflammatory disease. The gene encodes a protein named pyrin, which appears to play an important role in inflammatory pathways. Furthermore, pyrin, which is expressed in neutrophils, has been reported to interact with proline-serine-threonine phosphatase-interacting protein 1 (PSTPIP1) and actin proteins. However, the relations between pyrin and PSTPIP1 during the cell migration have not yet been elucidated. In the present study, we constructed a cell migration assay method using HL-60 cells. Pyrin-PSTPIP1 interactions were analysed by immunofluorescence staining in control, differentiated and differentiated-stimulated HL-60 cells. In stimulated cells, pyrin-polymerised actin, PSTPIP1-polymerised actin and pyrin-PSTPIP1 were found to be colocalised. Pyrin has been shown to be colocalised with actin and PSTPIP1 at the leading edge of the migrating cell. For the first time, PSTPIP1 was found to interact with dynamic actin and pyrin at the site of polarisation.
Insights
Familial Mediterranean Fever (FMF) is linked to MEFV gene mutations. This study reveals pyrin interacts with PSTPIP1 and actin during neutrophil migration, clarifying their roles in inflammation.
Area of Science:
- Immunology
- Cell Biology
- Genetics
Background:
- Familial Mediterranean Fever (FMF) is an auto-inflammatory disease caused by mutations in the Mediterranean Fever (MEFV) gene.
- The MEFV gene encodes pyrin, a protein crucial for inflammatory pathways, expressed in neutrophils.
- Pyrin's interaction with proline-serine-threonine phosphatase-interacting protein 1 (PSTPIP1) and actin is known, but its role in cell migration remains unclear.
Purpose of the Study:
- To investigate the interaction between pyrin and PSTPIP1 during cell migration.
- To elucidate the role of pyrin-PSTPIP1 complex in the context of cell migration dynamics.
Main Methods:
- Development of a cell migration assay using HL-60 cells.
- Immunofluorescence staining to analyze pyrin-PSTPIP1 interactions in control, differentiated, and stimulated HL-60 cells.
Main Results:
- Pyrin, PSTPIP1, and polymerized actin colocalized in stimulated HL-60 cells.
- Pyrin was observed to colocalize with actin and PSTPIP1 at the leading edge of migrating cells.
- PSTPIP1 was found to interact with dynamic actin and pyrin at the cell's polarization site.
Conclusions:
- This study demonstrates the colocalization of pyrin, PSTPIP1, and actin during neutrophil migration.
- The findings provide novel insights into the interaction of pyrin and PSTPIP1 at the leading edge of migrating cells.
- This research clarifies the molecular interactions underlying cell migration in the context of FMF and related inflammatory processes.
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