Proposed model for Regulation of BMP Activity by DDR2. (IMAGE)

Maximum Academic Press

Proposed model for Regulation of BMP Activity by DDR2.

Caption

Proposed model for Regulation of BMP Activity by DDR2. After binding collagen, DDR2 alone or together with collagen-binding β1 integrins stabilizes YAP/TAZ nuclear accumulation. This is accomplished in part by inhibiting YAP S127 phosphorylation possibly by inhibiting LATS1/2, thereby inhibiting cytoplasmic degradation, and could also involve increased actin polymerization and cytoskeletal stiffening leading to increased nuclear YAP/TAZ retention. BMP2 stimulates SMAD1/5/9 phosphorylation thereby promoting interaction with SMAD4 and nuclear accumulation of an R-SMAD-SMAD4 complex. In the nucleus, the WW1 domain of YAP binds and stabilizes the R-SMAD-SMAD4 complex to stimulate BMP-dependent transcription of genes necessary for cartilage and bone formation.

Credit

Bone Research

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