
Binding of AP2 to Sorting Signals Is Modulated by AP2 Phosphorylation
Feb 23, 2001 · Here we show that in vitro binding of AP2 to sorting signals, which is one of the initial steps in receptor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was phosphorylated by incubating purified AP2 in the presence of ATP and dephosphorylated by incubation with alkaline phosphatase.
Binding of AP2 to sorting signals is modulated by AP2 ... - PubMed
Feb 23, 2001 · Here we show that in vitro binding of AP2 to sorting signals, which is one of the initial steps in receptor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was phosphorylated by incubating purified AP2 in the presence of ATP and dephosphorylated by incubation with alkaline phosphatase.
Phosphorylation of the AP2 μ subunit by AAK1 mediates high …
We propose that phosphorylation of the AP2 μ2 subunit by AAK1 ensures high affinity binding of AP2 to sorting signals of cargo membrane proteins during the initial steps of receptor-mediated endocytosis.
Adaptor protein complexes and intracellular transport - PMC
The best-characterized sorting signals are tyrosine-based (YXXØ) and dileucine-based ([DE]XXXL[LI]) signals (X is any amino acid and Ø is a bulky hydrophobic amino acid, i.e. leucine, isoleucine, methionine, valine or phenylalanine), which are recognized by AP-1, AP-2 and AP-3.
An endocytic YXXΦ (YRRF) cargo sorting motif in the ... - PubMed
Via a tyrosine-based sorting motif YXXΦ in their cytoplasmic tails, they link the bound cargo to the cellular adapter protein-2 (AP2), thereby sorting it into clathrin-triskelion-coated pits for accelerated endocytosis.
Synaptic vesicle morphology: a case of protein sorting?
AP2 in synaptic vesicle endocytosis. The clathrin adaptor protein complex AP2 is a major protein–protein interaction hub that coordinates cargo sorting, accessory protein binding, and membrane internalization during endocytosis (Figure 1c) [15–18]. It internalizes transmembrane proteins by recognizing two sorting signals, that is, tyrosine ...
Here we show that in vitro binding of AP2 to sorting signals, which is one of the initial steps in recep-tor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was phosphorylated by incubat-ing purified AP2 in the presence of ATP and dephospho-rylated by incubation with alkaline phosphatase.
Binding of AP2 to Sorting Signals Is Modulated by AP2 Phosphorylation
Mar 1, 2001 · Here we show that in vitro binding of AP2 to sorting signals, which is one of the initial steps in receptor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was...
AP2 has been shown to bind to protein cargo through Yxxf-sorting motifs via the C-terminal subdo- main of its 2 subunit (C- 2, residues 157–435) (Ohno et al., 1995; Owen and Evans, 1998). The binding to acidic dileucine motifs is a point of contention in the literature.
Phosphatidylinositol-(4,5)-Bisphosphate Regulates Sorting Signal ...
May 27, 2005 · Recent studies on the function of AP2 have demonstrated that phosphorylation of the AP2 μ2 subunit modulates its function, with phosphorylation being a trigger for high-affinity binding of tyrosine-based sorting signals (Ricotta et al., 2002).