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Characterizing the function-related specific assembly pattern of matrix metalloproteinase-14 by dSTORM imaging
Dian Ge1, Junling Chen1, Zhiyong Zhao1
1Improve-WUST Joint Laboratory of Advanced Technology for Point-of-Care Testing and Precision Medicine, School of Chemistry & Chemical Engineering, Wuhan University of Science and Technology, 947 Heping Street, Wuhan, Hubei, 430081, China.
Talanta
|April 27, 2023
Summary
Matrix metalloproteinase-14 (MMP14) aggregates on cell membranes, coordinating cell migration. Its clustering increases with hydrolysis efficiency and co-localization with substrate PTK7 on highly migratory cells.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Matrix metalloproteinase-14 (MMP14) is a transmembrane enzyme regulating cell migration and cancer metastasis.
- Understanding MMP14's single-molecule function requires detailed knowledge of its spatial organization.
Purpose of the Study:
- To characterize the single-molecule distribution and spatial assembly of MMP14 on cell membranes.
- To investigate the relationship between MMP14 localization, migratory capacity, and substrate interaction.
Main Methods:
- Development and application of aptamer probes for MMP14 labeling.
- Utilizing direct Stochastic Optical Reconstruction Microscopy (dSTORM) for high-resolution imaging.
- Analyzing MMP14 co-localization with its substrate PTK7.
Main Results:
- MMP14 predominantly forms clusters on cell membranes.
- MMP14 clustering is more pronounced in high-migratory cells and correlates with enhanced hydrolysis efficiency.
- Significant co-localization of MMP14 with PTK7 was observed, decreasing as cell migration weakens.
Conclusions:
- MMP14 spatial organization, particularly its clustering and co-localization with PTK7, is crucial for coordinating cell migration.
- This study provides insights into MMP14's role in cell migration and cancer metastasis at the single-molecule level.
