[HTML][HTML] Tyrosine 537 within the Na+, K+-ATPase α-subunit is essential for AP-2 binding and clathrin-dependent endocytosis
SC Doné, IB Leibiger, R Efendiev, AI Katz… - Journal of Biological …, 2002 - ASBMB
In renal epithelial cells endocytosis of Na+, K+-ATPase molecules is initiated by
phosphorylation of its α 1-subunit, leading to activation of phosphoinositide 3-kinase and
adaptor protein-2 (AP-2)/clathrin recruitment. The present study was performed to establish
the identity of the AP-2 recognition domain (s) within the Na+, K+-ATPase α 1-subunit. We
identified a conserved sequence (Y 537 LEL) within the α 1-subunit that represents an AP-2
binding site. Binding of AP-2 to the Na+, K+-ATPase α 1-subunit in response to dopamine …
phosphorylation of its α 1-subunit, leading to activation of phosphoinositide 3-kinase and
adaptor protein-2 (AP-2)/clathrin recruitment. The present study was performed to establish
the identity of the AP-2 recognition domain (s) within the Na+, K+-ATPase α 1-subunit. We
identified a conserved sequence (Y 537 LEL) within the α 1-subunit that represents an AP-2
binding site. Binding of AP-2 to the Na+, K+-ATPase α 1-subunit in response to dopamine …