A dileucine motif is involved in plasma membrane expression and endocytosis of rat sodium taurocholate cotransporting polypeptide (Ntcp).

The sodium taurocholate cotransporting polypeptide (Ntcp) is the major uptake transporter for bile salts into liver parenchymal cells, and PKC-mediated endocytosis was shown to regulate the number of Ntcp molecules at the plasma membrane. In this study, mechanisms of Ntcp internalization were analyzed by flow cytometry, immunofluorescence, and Western blot analyses in HepG2 cells. PKC activation induced endocytosis of Ntcp from the plasma membrane by ~30%.

Expression and localization of atypical PKC isoforms in liver parenchymal cells.

Members of all three classes of the protein kinase C (PKC) family including atypical PKCzeta (PKCzeta) are involved in central functions of liver parenchymal cells. However, expression and localization of PKCiota (PKCiota), the highly homologous atypical PKC (aPKC) isoform, in hepatocytes is unknown to date. PKCzeta and PKCiota were cloned from human and rat liver and fused to fluorescent protein tags (YFP).