Additional file 1: of The small GTPase Rab5c is a key regulator of trafficking of the CD93/Multimerin-2/β1 integrin complex in endothelial cell adhesion and migration
Additional file 1: of The small GTPase Rab5c is a key regulator of trafficking of the CD93/Multimerin-2/β1 integrin complex in endothelial cell adhesion and migration
Figure S1. Small vesicles containing CD93 colocalize with caveolin-1 in early spreading ECs. Figure S2. Disruption of the actin cytoskeleton impairs CD93 intracellular trafficking. Figure S3. Microtubule cytoskeleton disruption has no effects on CD93 intracellular trafficking. Figure S4. CD93 trafficking does not depend on transport from or to the Golgi complex. Figure S5. CD93 is colocalized with MMRN2 in spreading HDBECs. Figure S6. CD93 colocalizes strongly with Rab5 and slightly with Rab11, but not with Rab7. Figure S7. Rab5c is the predominant isoform in HUVECs. Figure S8. Rab5c regulates CD93 recycling to the cell surface. Figure S9. β1 integrin protein levels decrease at the leading edge of migrating Rab5c-silenced ECs. Figure S10. In CD93 silenced ECs, large Rab5c+ve vesicles form regularly. (PDF 2570 kb)
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