| Literature DB >> 36205720 |
Olivier Destaing1, Catherine Picart2,3, Corinne Albiges-Rizo1, Amaris Guevara-Garcia1,2,3, Laure Fourel1, Ingrid Bourrin-Reynard1, Adria Sales2,3, Christiane Oddou1, Mylène Pezet1, Olivier Rossier4, Paul Machillot2,3, Line Chaar1, Anne-Pascale Bouin1, Gregory Giannone4.
Abstract
The spatial organization of cell-surface receptors is fundamental for the coordination of biological responses to physical and biochemical cues of the extracellular matrix. How serine/threonine kinase receptors, ALK3-BMPRII, cooperate with integrins upon BMP2 to drive cell migration is unknown. Whether the dynamics between integrins and BMP receptors intertwine in space and time to guide adhesive processes is yet to be elucidated. We found that BMP2 stimulation controls the spatial organization of BMPRs by segregating ALK3 from BMPRII into β3 integrin-containing focal adhesions. The selective recruitment of ALK3 to focal adhesions requires β3 integrin engagement and ALK3 activation. BMP2 controls the partitioning of immobilized ALK3 within and outside focal adhesions according to single-protein tracking and super-resolution imaging. The spatial control of ALK3 in focal adhesions by optogenetics indicates that ALK3 acts as an adhesive receptor by eliciting cell spreading required for cell migration. ALK3 segregation from BMPRII in integrin-based adhesions is a key aspect of the spatio-temporal control of BMPR signaling.Entities:
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Year: 2022 PMID： 36205720 PMCID： PMC9552562 DOI： 10.1083/jcb.202107110
Source DB: PubMed Journal: J Cell Biol ISSN： 0021-9525 Impact factor: 8.077