INVESTIGADORES
REY Osvaldo
artículos
Título:
Rapid protein kinase D translocation in response to G protein-coupled receptor activation. Dependence on protein kinase C.
Autor/es:
REY O, YOUNG SH, CANTRELL D, ROZENGURT E.
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Referencias:
Año: 2001 p. 32616 - 32626
ISSN:
0021-9258
Resumen:
Protein kinase D (PKD)/protein kinase C (PKC) mu is a serine/threonine
protein kinase that can be activated by physiological stimuli like
growth factors, antigen-receptor engagement and G protein-coupled
receptor (GPCR) agonists via a phosphorylation-dependent mechanism that
requires PKC activity. In order to investigate the dynamic mechanisms
associated with GPCR signaling, the intracellular translocation of a
green fluorescent protein-tagged PKD was analyzed by real-time
visualization in fibroblasts and epithelial cells stimulated with
bombesin, a GPCR agonist. We found that bombesin induced a rapidly
reversible plasma membrane translocation of green fluorescent
protein-tagged PKD, an event that can be divided into two distinct
mechanistic steps. The first step, which is exclusively mediated by the
cysteine-rich domain in the N terminus of PKD, involved its
translocation from the cytosol to the plasma membrane. The second step,
i.e. the rapid reverse translocation of PKD from the plasma membrane to
the cytosol, required its catalytic domain and surprisingly PKC
activity. These findings provide evidence for a novel mechanism by
which PKC coordinates the translocation and activation of PKD in
response to bombesin-induced GPCR activation.