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Vasopressin‐induced intracellular redistribution of protein kinase D in intestinal epithelial cells
Author(s) -
Rey Osvaldo,
Zhukova Elena,
SinnettSmith James,
Rozengurt Enrique
Publication year - 2003
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.10323
Subject(s) - microbiology and biotechnology , protein kinase c , intracellular , cytosol , signal transduction , protein kinase a , biology , g protein coupled receptor , kinase , chemistry , biochemistry , enzyme
The spatio‐temporal changes of signaling molecules in response to G protein‐coupled receptors (GPCR) stimulation is a poorly understood process in intestinal epithelial cells. Here we investigate the dynamic mechanisms associated with GPCR signaling in living rat intestinal epithelial cells by characterizing the intracellular translocation of protein kinase D (PKD), a serine/threonine protein kinase involved in mitogenic signaling in intestinal epithelial cells. Analysis of the intracellular steady‐state distribution of green fluorescent protein (GFP)‐tagged PKD indicated that in non‐stimulated IEC‐18 cells, GFP‐PKD is predominantly cytoplasmic. However, cell stimulation with the GPCR agonist vasopressin induces a rapid translocation of GFP‐PKD from the cytosol to the plasma membrane that is accompanied by its activation via protein kinase C (PKC)‐mediated process and posterior plasma membrane dissociation. Subsequently, active PKD is imported into the nuclei where it transiently accumulates before being exported into the cytosol by a mechanism that requires a competent Crm1 nuclear export pathway. These findings provide evidence for a mechanism by which PKC coordinates in intestinal epithelial cells the translocation and activation of PKD in response to vasopressin‐induced GPCR activation. J. Cell. Physiol. 196: 483–492, 2003. © 2003 Wiley‐Liss, Inc.