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Vol. 12, Issue 12, 4114-4128, December 2001
Division of Biology, Section of Cell and Developmental Biology,
University of California, San Diego, La Jolla, California 92093-0347
We isolated a temperature-sensitive mutant, hrd4-1,
deficient in ER-associated degradation (ERAD). The HRD4
gene was identical to NPL4, a gene previously implicated
in nuclear transport. Using a diverse set of substrates and direct
ubiquitination assays, our analysis revealed that
HRD4/NPL4 is required for a poorly characterized step in
ERAD after ubiquitination of target proteins but before their
recognition by the 26S proteasome. Our data indicate that this lack of
proteasomal processing of ubiquitinated proteins constitutes the
primary defect in hrd4/npl4 mutant cells and explains the diverse set of hrd4/npl4 phenotypes. We also found
that each member of the Cdc48p-Ufd1p-Npl4p complex is individually
required for ERAD.
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