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. Author manuscript; available in PMC: 2013 Apr 12.
Published in final edited form as: Physiology (Bethesda). 2010 Oct;25(5):280–292. doi: 10.1152/physiol.00022.2010

FIGURE 4. Mechanisms by which endocytosis is controlled by phosphorylation.

FIGURE 4

A: phosphorylation of residues within or near internalization signals can enhance (AQP4) or inhibit (GABA-A receptor) their interaction with endocytotic machinery. B: in transport proteins, like the Na-K-ATPase (see text), phosphorylation at sites other than the endocytotic signal can create interaction sites for proteins that are indirectly involved in endocytosis. C: endocytotic machinery is also regulated by phosphorylation. For example, the binding site for tyrosine-based internalization signals on the AP-2 complex (mu subunit) is exposed on phosphorylation by AAK1 (or by PIP2 association).