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. 2019 Oct 25;294(49):18881–18897. doi: 10.1074/jbc.RA119.010110

Figure 5.

Figure 5.

SRCR domain of SCARA1 recognizes the SPEC domain of spectrin. A, SPEC domain of spectrin binds to hSCARA1 in the presence of Ca2+, whereas SH3 and the EF hand domain of spectrin have no binding to hSCARA1. Sumo is applied as a control. B, SPEC domain of spectrin blocks the binding of the CL–SRCR fragment of hSCARA1 to the dead Jurkat cells, whereas the SH3 and the EF hand domains have no inhibition to the binding. C, SPEC domain of spectrin blocks the binding of the CL–SRCR fragment of hSCARA1 to the dead HEK293 cells, whereas the SH3 and the EF hand domains have no inhibition to the binding. D, SPEC domain of spectrin blocks the binding of the CL–SRCR fragment of mSCARA1 to the dead NIH 3T3 cells, whereas the SH3 and the EF hand domains have no inhibition to the binding. E, CL–SRCR fragments with the Ca2+-binding site mutations have no binding to the SPEC domain of spectrin. F, SPEC9e and SPEC11e from erythrocytic spectrin bind to SCARA1 in the presence of Ca2+. The SH3 domain and Sumo are applied as controls. G, SPECe domains from erythrocytic spectrin block the binding of the CL–SRCR fragment of hSCARA1 to dead Jurkat cells. H, binding affinities between the SCARA1 fragments (SRCR, CL–SRCR, and 5J0J–SRCR) with SPEC1 in the presence of Ca2+. GFP is applied as a control.