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Vol. 13, Issue 5, 1566-1581, May 2002
Department of Biology, The Johns Hopkins University, Baltimore,
Maryland 21218
Quality control of protein biosynthesis requires ER-retention and
ER-associated degradation (ERAD) of unassembled/misfolded molecules.
Although some evidence exists for the organization of the ER into
functionally distinct membrane domains, it is unknown if such domains
are involved in the retention and ERAD of unassembled proteins. Here,
it is shown that unassembled MHC class I molecules are retained in the
ER without accumulating at ER-exit sites or in the ERGIC of
2m
/ cells. Furthermore, these
molecules did not cluster in the ER membrane and appeared to be highly
mobile even when ERAD or their association with calnexin were
inhibited. However, upon ATP depletion, they were reversibly segregated
into an ER membrane domain, distinct from ER exit sites, which included
calnexin and COPII, but not the ERGIC marker protein p58. This quality
control domain was also observed upon prolonged inhibition of
proteasomes. Microtubules were required for its appearance. Segregation
of unfolded proteins, ER-resident chaperones, and COPII may be a
temporal adaptation to cell stress.
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