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Integrin-based adhesion compartmentalizes ALK3 of the BMPRII to control cell adhesion and migration
Amaris Guevara-Garcia1,2,3, Laure Fourel1, Ingrid Bourrin-Reynard1
1Institute for Advanced Biosciences, Institut National de la Santé et de la Recherche Médicale U1209, Centre National de La Recherche Scientifique 5309, Université Grenoble Alpes, Grenoble, France.
The Journal of Cell Biology
|October 7, 2022
Summary
Bone morphogenetic protein 2 (BMP2) stimulation spatially organizes bone morphogenetic protein receptors (BMPRs). ALK3 segregates from BMPRII into focal adhesions, regulating cell migration.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Cell-surface receptor organization is crucial for biological responses to extracellular matrix cues.
- The interplay between serine/threonine kinase receptors (ALK3-BMPRII) and integrins in response to BMP2 for cell migration remains unclear.
Purpose of the Study:
- To investigate how ALK3 and BMPRII cooperate with integrins upon BMP2 stimulation.
- To elucidate the spatio-temporal dynamics between integrins and BMP receptors in guiding adhesive processes.
Main Methods:
- Single-protein tracking
- Super-resolution imaging
- Optogenetics
- Biochemical assays
Main Results:
- BMP2 stimulation induces spatial segregation of ALK3 and BMPRII into β3 integrin-containing focal adhesions.
- ALK3 recruitment to focal adhesions necessitates β3 integrin engagement and ALK3 activation.
- Optogenetic spatial control of ALK3 in focal adhesions demonstrates its role as an adhesive receptor promoting cell spreading and migration.
Conclusions:
- BMP2 signaling is spatiotemporally controlled by the segregation of ALK3 from BMPRII within integrin-based adhesions.
- ALK3 functions as an adhesive receptor, mediating cell migration through focal adhesion dynamics.
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