Little is known about the identity of endoplasmic reticulum (ER) export sig
nals and how they are used to regulate the number of proteins on the cell s
urface. Here, we describe two ER export signals that profoundly altered the
steady-state distribution of potassium channels and were required for chan
nel localization to the plasma membrane. When transferred to other potassiu
m channels or a G protein-coupled receptor, these ER export signals increas
ed the number of functional proteins on the cell surface. Thus, ER export o
f membrane proteins is not necessarily limited by folding or assembly, but
may be under the control of specific export signals.