β2-adrenergic receptor lysosomal trafficking is regulated by ubiquitination of lysyl residues in two distinct receptor domains
K Xiao, SK Shenoy - Journal of Biological Chemistry, 2011 - ASBMB
Agonist stimulation of the β 2-adrenergic receptors (β 2 ARs) leads to their ubiquitination
and lysosomal degradation. Inhibition of lysosomal proteases results in the stabilization and
retention of internalized full-length β 2 ARs in the lysosomes, whereas inhibition of
proteasomal proteases stabilizes newly synthesized β 2 ARs in nonlysosomal
compartments. Additionally, a lysine-less β 2 AR (0K-β 2 AR) that is deficient in
ubiquitination and degradation is not sorted to lysosomes unlike the WT β 2 AR, which is …
and lysosomal degradation. Inhibition of lysosomal proteases results in the stabilization and
retention of internalized full-length β 2 ARs in the lysosomes, whereas inhibition of
proteasomal proteases stabilizes newly synthesized β 2 ARs in nonlysosomal
compartments. Additionally, a lysine-less β 2 AR (0K-β 2 AR) that is deficient in
ubiquitination and degradation is not sorted to lysosomes unlike the WT β 2 AR, which is …
