Reduced VEGFR2 availability at the plasma membrane could thus diminish response to exogenously added VEGFA
Reduced VEGFR2 availability at the plasma membrane could thus diminish response to exogenously added VEGFA. dimerization and transautophosphorylation of several important tyrosine residues present within its cytoplasmic kinase domain1. Upon activation, VEGFR2 enters the endosomelysosome system through incorporation into clathrincoated vesicles and trafficking to early endosomal vesicular compartments4. Ubiquitination of VEGFR2 acts as an endosomal sorting signal by binding to the ubiquitininteracting motif of ESCRT0 components, Hrs and STAM4, 5, 6. Internalized VEGFR2 can recycle back to the plasma membrane or be committed to get lysosomal degradation6, 7. Ubiquitination is a powerful protein customization that coordinates receptor trafficking, recycling SRPKIN-1 and degradation8. Reversibilty of ubiquitination is credited to the action of deubiquitinating enzymes (DUBs)8. These enzymes thus play a distinct but crucial role in receptor tyrosine kinase trafficking and turnover8.…