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J. Biol. Chem., Vol. 277, Issue 40, 37702-37710, October 4, 2002
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From the The mechanisms by which
glucose may affect protein kinase C (PKC) activity in the pancreatic
islet
Dynamics of Glucose-induced Membrane Recruitment of Protein
Kinase C
II in Living Pancreatic Islet -Cells*,
§¶
**,,,
Henry Wellcome Signalling Laboratories and
the Department of Biochemistry, University of Bristol, Bristol BS8
1TD, United Kingdom, the § Department of Biomedical Sciences
and CNR Centre for Study of Biological Membranes, University of Padova,
Viale G. Colombo 3, 35121 Padova, Italy, and the ¶ Department of
Experimental and Diagnostic Medicine Section of the General Pathology
and Interdisciplinary Center for the Study of Inflammation (ICSI),
University of Ferrara, Via Borsari, 46 44100 Ferrara, Italy
-cell are presently unclear. By developing adenovirally
expressed chimeras encoding fusion proteins between green fluorescent
protein and conventional (II), novel (
), or atypical (
)
PKCs, we show that glucose selectively alters the subcellular
localization of these enzymes dynamically in primary islet and MIN6
-cells. Examined by laser scanning confocal or total internal
reflection fluorescence microscopy, elevated glucose concentrations
induced oscillatory translocations of PKCII to spatially confined
regions of the plasma membrane. Suggesting that increases in free
cytosolic Ca2+ concentrations
([Ca2+]c) were primarily responsible,
prevention of [Ca2+]c increases with EGTA or
diazoxide completely eliminated membrane recruitment, whereas elevation
of cytosolic [Ca2+]c with KCl or tolbutamide
was highly effective in redistributing PKCII both to the plasma
membrane and to the surface of dense core secretory vesicles. By
contrast, the distribution of PKC·EGFP, which binds diacylglycerol
but not Ca2+, was unaffected by glucose. Measurement of
[Ca2+]c immediately beneath the plasma
membrane with a ratiometric "pericam," fused to synaptic
vesicle-associated protein-25, revealed that depolarization induced
significantly larger increases in [Ca2+]c in
this domain. These data demonstrate that nutrient stimulation of
-cells causes spatially and temporally complex changes in the
subcellular localization of PKCII, possibly resulting from the
generation of Ca2+ microdomains. Localized changes in
PKCII activity may thus have a role in the spatial control of
insulin exocytosis.
*
This work was supported by grants from the Human Frontiers
Sciences Program, the Medical Research Council (UK), The Wellcome Trust, the Biotechnology and Biological Research Council, Diabetes UK,
the European Union, the Italian "Telethon" (Project No. 1250), the
Italian University and Health Ministries, the Italian Space Agency, The
Italian National Research Council, The Armenise Harvard Foundation, and
the Italian Association for Cancer Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains movies for Figs.
2-5.
Both authors contributed equally to this work.
**
Recipient of an EMBO short-term fellowship.
To whom correspondence should be addressed. Tel.:
44-117-954-6491; Fax: 44-117-928-8274; E-mail:
g.a.rutter@bris.ac.uk.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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