Nearly all members of the inwardly rectifying potassium (Kir) channel family share a
cytoplasmic domain structure that serves as an unusual AP-1 clathrin adaptor-dependent …

Surface expression of ion channels and receptors often depends on intrinsic sequence
motifs that control their intracellular transport along the secretory pathway. Although …

The inward rectifying potassium channel, Kir2. 1, is selected as cargo at the trans-Golgi
network (TGN) for export to the cell surface through a unique signal-dependent interaction …

Mechanisms that are responsible for sorting newly synthesized proteins for traffic to the cell
surface from the Golgi are poorly understood. Here, we show that the potassium channel …

The localization and density of Kir2. 3 channels are influenced by the balance between PDZ
protein interaction at the cell surface and routing into the endocytic pathway. Here, we …

Traffic of integral membrane proteins along the secretory pathway is not simply a default
process but can be selective. Such selectivity is achieved by sequence information within …

N-and C-terminal cytoplasmic domains of inwardly rectifying K (Kir) channels control the ion-
permeation pathway through diverse interactions with small molecules and protein ligands …

Regulation of inwardly rectifying potassium channels by intracellular ligands couples cell
membrane excitability to important signaling cascades and metabolic pathways. We …

Integral membrane proteins are sorted via the secretory pathway. It was proposed that this
pathway is non‐selective provided that the cargo protein is properly assembled and lacks an …

K ATP channels are unique in requiring two distinct subunits (Kir6. 2, a potassium channel
subunit) and SUR1 (an ABC protein) for generation of functional channels. To examine the …