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. Author manuscript; available in PMC: 2021 Mar 1.
Published in final edited form as: J Thromb Haemost. 2019 Dec 30;18(3):693–705. doi: 10.1111/jth.14687

Figure 1: The atypical C1 domain plays an important role for CDGI/Rap1-mediated platelet aggregation.

Figure 1:

(A) Schematic representation of CDGI domain structure. Shown are full-length CDGI protein (609 residues), a C-terminally truncated CDGI that contains all functional domains (1–551), CDGI lacking the C1 domain (CDGIΔC1; 1–499) and the isolated C1 domain (492–551). (B, C) Aggregation and Rap1 activation response in platelets expressing CDGIΔC1. Platelets isolated from wild-type (+/+), CDGI heterozygous (+/−), CDGI knockout (−/−) and chimeric mice expressing CDGIΔC1 (ΔC1)13 were activated with convulxin (GPVI agonist) and aggregation was recorded over time (B). At the indicated time points, platelets were lysed and Rap1-GTP levels were determined (C). Results are representative of 3 independent experiments. (D) Nucleotide exchange activity assay. Purified CDGI or CDGIΔC1 protein was added to Rap1B in the presence of BODIPY-GDP. The change in fluorescence intensity due to binding of BODIPY-GDP to Rap1B was measured over time. Results are representative of 5 independent experiments.