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Vol. 11, Issue 1, 217-226, January 2000
Biochemie-Zentrum Heidelberg, D-69120 Heidelberg, Germany
Unassembled immunoglobulin light chains expressed by the
mouse plasmacytoma cell line NS1 (
NS1) are degraded in
vivo with a half-life of 50-60 min in a way that closely resembles
endoplasmic reticulum (ER)-associated degradation (Knittler et
al., 1995). Here we show that the peptide aldehydes MG132 and
PS1 and the specific proteasome inhibitor lactacystin effectively
increased the half-life of NS1, arguing for a
proteasome-mediated degradation pathway. Subcellular fractionation and
protease protection assays have indicated an ER localization of
NS1 upon proteasome inhibition. This was independently
confirmed by the analysis of the folding state of NS1
and size fractionation experiments showing that the immunoglobulin
light chain remained bound to the ER chaperone BiP when the
activity of the proteasome was blocked. Moreover, kinetic studies
performed in lactacystin-treated cells revealed a time-dependent
increase in the physical stability of the BiP-NS1 complex, suggesting that additional proteins are present in the older
complex. Together, our data support a model for ER-associated degradation in which both the release of a soluble nonglycosylated protein from BiP and its retrotranslocation out of the ER are tightly
coupled with proteasome activity.
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