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Vol. 11, Issue 8, 2577-2590, August 2000
Department of Biological Sciences, Carnegie Mellon
University, Pittsburgh, Pennsylvania 15213
Recent evidence suggests a regulatory connection between cell
volume, endoplasmic reticulum (ER) export, and stimulated Golgi-to-ER transport. To investigate the potential role of protein kinases we
tested a panel of protein kinase inhibitors for their effect on these
steps. One inhibitor, H89, an isoquinolinesulfonamide that is commonly
used as a selective protein kinase A inhibitor, blocked both ER export
and hypo-osmotic-, brefeldin A-, or nocodazole-induced Golgi-to-ER transport. In contrast, H89 did not block the constitutive ER Golgi-intermediate compartment (ERGIC)-to-ER and Golgi-to-ER traffic
that underlies redistribution of ERGIC and Golgi proteins into the ER
after ER export arrest. Surprisingly, other protein kinase A
inhibitors, KT5720 and H8, as well as a set of protein kinase C
inhibitors, had no effect on these transport processes. To test whether
H89 might act at the level of either the coatomer protein (COP)I or the
COPII coat protein complex we examined the localization of 
COP and
Sec13 in H89-treated cells. H89 treatment led to a rapid loss of
Sec13-labeled ER export sites but COP localization to the Golgi was
unaffected. To further investigate the effect of H89 on COPII we
developed a COPII recruitment assay with permeabilized cells and found
that H89 potently inhibited binding of exogenous Sec13 to ER export
sites. This block occurred in the presence of
guanosine-5'-O-(3-thio)triphosphate, suggesting that
Sec13 recruitment is inhibited at a step independent of the activation
of the GTPase Sar1. These results identify a requirement for an
H89-sensitive factor(s), potentially a novel protein kinase, in
recruitment of COPII to ER export sites, as well as in stimulated but
not constitutive Golgi-to-ER transport.
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