TypeIVcollagenisanactivatingligandfortheadhesionG.pptVIP

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TypeIVcollagenisanactivatingligandfortheadhesionG.ppt

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TypeIVcollagenisanactivatingligandfortheadhesionG.ppt

Type IV collagen is an activating ligand for the adhesion G protein–coupled receptor GPR126 by Kevin J. Paavola, Harwin Sidik, J. Bradley Zuchero, Michael Eckart, and William S. Talbot Sci. Signal. Volume 7(338):ra76-ra76 August 12, 2014 ?2014 by American Association for the Advancement of Science Type IV collagen binds specifically to the N-terminal region of Gpr126. Kevin J. Paavola et al., Sci. Signal. 2014;7:ra76 ?2014 by American Association for the Advancement of Science Type IV collagen stimulates cAMP signaling in cells expressing Gpr126. Kevin J. Paavola et al., Sci. Signal. 2014;7:ra76 ?2014 by American Association for the Advancement of Science A region of Gpr126 containing CUB and PTX domains mediates the high-affinity interaction with type IV collagen. Kevin J. Paavola et al., Sci. Signal. 2014;7:ra76 ?2014 by American Association for the Advancement of Science The N-terminal region of Gpr126 inhibits receptor signaling activity. Kevin J. Paavola et al., Sci. Signal. 2014;7:ra76 ?2014 by American Association for the Advancement of Science The gpr126st86 mutation truncates Gpr126 after the PTX domain and disrupts myelination and ear development. Kevin J. Paavola et al., Sci. Signal. 2014;7:ra76 ?2014 by American Association for the Advancement of Science Type IV collagen binds specifically to the N-terminal region of Gpr126.(A) Schematic diagram showing the conserved domains of Gpr126 including signal peptide (SP), CUB (complement, Uegf, Bmp1), pentraxin (PTX), hormone-binding domain (HBD), GAIN domain, and 7TM region in the wild-type protein and the corresponding N-terminal fusion protein Gpr126-NT-Fc. The amino acids mediating the autocatalytic cleavage of the GAIN domain are noted (HLT), and the position of the cleavage is indicated by the line in the GAIN domain. (B and C) Conditioned medium containing Gpr126-NT-Fc fusion protein was mixed with biotinylated collagen or BSA and incubated with streptavidin-agarose. Interactions (B) were detected by imm